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Conserved domains on  [gi|28559083|ref|NP_062831|]
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CTP synthase 2 [Homo sapiens]

Protein Classification

CTP synthase( domain architecture ID 11476640)

cytidine triphosphate (CTP) synthase catalyzes the conversion of UTP to CTP in the last committed step in pyrimidine nucleotide biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-557 0e+00

CTP synthase


:

Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 930.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083    1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFV 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  161 EAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  241 VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLfKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  321 LEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCL 400
Cdd:PLN02327 320 LLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  401 GMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH 480
Cdd:PLN02327 400 GMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRH 479

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28559083  481 RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAYLQQ 557
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-557 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 930.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083    1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFV 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  161 EAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  241 VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLfKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  321 LEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCL 400
Cdd:PLN02327 320 LLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  401 GMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH 480
Cdd:PLN02327 400 GMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRH 479

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28559083  481 RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAYLQQ 557
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-547 0e+00

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 831.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:COG0504   1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKvpvdgnKEEPQICVIELGGTIGDIEGMPFV 160
Cdd:COG0504  81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAE------ESGADVVIVEIGGTVGDIESLPFL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 161 EAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 241 VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSAsnlLFKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPD---LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 321 LEHSALAINHKLNLMYIDSIDLEKitetedpvkfHEAWQKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCL 400
Cdd:COG0504 312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 401 GMQLAVIEFARNCLNLKDADSTEFRPNAPVPlVID-MPE-HNPGNLGGTMRLGIRRTVFKtENSILRKLYGDvPFIEERH 478
Cdd:COG0504 382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCKLK-PGTLAAEAYGK-EEISERH 458

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28559083 479 RHRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAA 547
Cdd:COG0504 459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-546 0e+00

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 783.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083     1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083    81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKvpvdgnKEEPQICVIELGGTIGDIEGMPFV 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAK------ISGPDVVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   161 EAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   241 VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLpigDSASNLLFKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL---NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   321 LEHSALAINHKLNLMYIDSIDLEkitetEDPVKFHEAwqklckADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLE-----EEGVEFLKG------LDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   401 GMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPEHNP-GNLGGTMRLGIRRTVFKtENSILRKLYGDvPFIEERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVYERHR 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28559083   480 HRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLA 546
Cdd:TIGR00337 459 HRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 2-272 0e+00

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 554.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083     2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083    82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKvpvdgnKEEPQICVIELGGTIGDIEGMPFVE 161
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK------EVGPDVVIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   162 AFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 28559083   242 ICIHDVSSTYRVPVLLEEQSIVKYFKERLHL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 2-268 0e+00

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 532.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:cd03113   1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKVPvdgnkeEPQICVIELGGTIGDIEGMPFVE 161
Cdd:cd03113  81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 162 AFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234

                       250       260
                ....*....|....*....|....*..
gi 28559083 242 ICIHDVSSTYRVPVLLEEQSIVKYFKE 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
 
Name Accession Description Interval E-value
PLN02327 PLN02327
CTP synthase
 1-557 0e+00

CTP synthase


Pssm-ID: 215186 [Multi-domain]  Cd Length: 557  Bit Score: 930.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083    1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PLN02327   1 MKYVLVTGGVVSGLGKGVTASSIGVLLKACGLRVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFV 160
Cdd:PLN02327  81 TLTRDNNITTGKIYQSVIEKERRGDYLGKTVQVVPHITDAIQEWIERVAKIPVDGKEGPADVCVIELGGTVGDIESMPFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  161 EAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PLN02327 161 EALRQFSFRVGPGNFCLIHVSLVPVLGVVGEQKTKPTQHSVRGLRALGLTPHILACRSTKPLEENVKEKLSQFCHVPAEN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  241 VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLfKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PLN02327 241 ILNLHDVSNIWHVPLLLRDQKAHEAILKVLNLLSVAREPDLE-EWTARAESCDNLTEPVRIAMVGKYTGLSDSYLSVLKA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  321 LEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCL 400
Cdd:PLN02327 320 LLHASVACSRKLVIDWVAASDLEDETAKETPDAYAAAWKLLKGADGILVPGGFGDRGVEGKILAAKYARENKVPYLGICL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  401 GMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRH 480
Cdd:PLN02327 400 GMQIAVIEFARSVLGLKDANSTEFDPETPNPCVIFMPEGSKTHMGGTMRLGSRRTYFQTPDCKSAKLYGNVSFVDERHRH 479

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28559083  481 RFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAYLQQ 557
Cdd:PLN02327 480 RYEVNPEMVPRLEKAGLSFVGKDETGRRMEIVELPSHPFFVGVQFHPEFKSRPGKPSPLFLGLIAAASGQLDAVLNS 556
pyrG PRK05380
CTP synthetase; Validated
 1-547 0e+00

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 831.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083    1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:PRK05380   2 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAkvpvdgnkEEPQICVIELGGTIGDIEGMPFV 160
Cdd:PRK05380  82 NLTKYNNVTTGKIYSSVIEKERRGDYLGKTVQVIPHITDEIKERILAAG--------TDADVVIVEIGGTVGDIESLPFL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  161 EAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:PRK05380 154 EAIRQLRLELGRENVLFIHLTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEEKRKIALFCNVPEEA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  241 VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSAsnlLFKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:PRK05380 234 VISAPDVDSIYEVPLLLHEQGLDDIVLERLGLEAPEPD---LSEWEELVERLKNPKGEVTIALVGKYVELPDAYKSVIEA 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  321 LEHSALAINHKLNLMYIDSIDLEKITETEdpvkfheawqKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCL 400
Cdd:PRK05380 311 LKHAGIANDVKVNIKWIDSEDLEEENVAE----------LLKGVDGILVPGGFGERGIEGKILAIRYARENNIPFLGICL 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  401 GMQLAVIEFARNCLNLKDADSTEFRPNAPVPlVID-MPE-HNPGNLGGTMRLGIRRTVFKtENSILRKLYGDvPFIEERH 478
Cdd:PRK05380 381 GMQLAVIEFARNVLGLEDANSTEFDPDTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCKLK-PGTLAAEIYGK-EEIYERH 457

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28559083  479 RHRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAA 547
Cdd:PRK05380 458 RHRYEVNNKYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPRRPHPLFAGFVKAA 526
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 1-547 0e+00

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 831.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:COG0504   1 TKYIFVTGGVVSSLGKGITAASLGRLLKARGLKVTIQKLDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKvpvdgnKEEPQICVIELGGTIGDIEGMPFV 160
Cdd:COG0504  81 NLSKANNVTTGQIYSSVIEKERRGDYLGKTVQVIPHITDEIKRRIRRAAE------ESGADVVIVEIGGTVGDIESLPFL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 161 EAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:COG0504 155 EAIRQLRLELGRENVLFIHVTLVPYIAAAGELKTKPTQHSVKELRSIGIQPDILVCRSERPLPEEIKRKIALFCNVPEEA 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 241 VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSAsnlLFKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:COG0504 235 VISAPDVDSIYEVPLMLHEQGLDEIVLKKLGLEAREPD---LSEWEELVERIKNPKKEVTIALVGKYVELPDAYKSVVEA 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 321 LEHSALAINHKLNLMYIDSIDLEKitetedpvkfHEAWQKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCL 400
Cdd:COG0504 312 LKHAGIANGVKVNIKWIDSEDLEE----------ENAEELLKGVDGILVPGGFGERGIEGKIAAIRYARENKIPFLGICL 381

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 401 GMQLAVIEFARNCLNLKDADSTEFRPNAPVPlVID-MPE-HNPGNLGGTMRLGIRRTVFKtENSILRKLYGDvPFIEERH 478
Cdd:COG0504 382 GMQLAVIEFARNVLGLEDANSTEFDPNTPHP-VIDlMPEqKDVSDLGGTMRLGAYPCKLK-PGTLAAEAYGK-EEISERH 458

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28559083 479 RHRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAA 547
Cdd:COG0504 459 RHRYEFNNEYREQLEKAGLVFSGTSPDGRLVEIVELPDHPWFVGVQFHPEFKSRPNRPHPLFRGFVKAA 527
PyrG TIGR00337
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ...
 1-546 0e+00

CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273021 [Multi-domain]  Cd Length: 525  Bit Score: 783.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083     1 MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDI 80
Cdd:TIGR00337   1 MKYIFVTGGVVSSLGKGITAASLGRLLKARGLNVTIIKIDPYINIDPGTMSPLQHGEVFVTDDGAETDLDLGHYERFLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083    81 NLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKvpvdgnKEEPQICVIELGGTIGDIEGMPFV 160
Cdd:TIGR00337  81 NLTRDNNITTGKIYSSVIEKERKGDYLGKTVQIIPHITNEIKDRILRVAK------ISGPDVVIVEIGGTVGDIESLPFL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   161 EAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQ 240
Cdd:TIGR00337 155 EAIRQFRVEVGRENVLFIHVTLVPYIAAAGEQKTKPTQHSVKELRSLGIQPDIIICRSSRPLDPNTKDKIALFCDVEEEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   241 VICIHDVSSTYRVPVLLEEQSIVKYFKERLHLpigDSASNLLFKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKA 320
Cdd:TIGR00337 235 VISAKDVSSIYEVPLLLLKQGLDDYLCRRLNL---NCDEADLSEWEQLVEKFANPKHEVTIGIVGKYVELKDAYLSVIEA 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   321 LEHSALAINHKLNLMYIDSIDLEkitetEDPVKFHEAwqklckADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCL 400
Cdd:TIGR00337 312 LKHAGAKLDTKVNIKWIDSEDLE-----EEGVEFLKG------LDGILVPGGFGERGVEGKILAIKYARENNIPFLGICL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   401 GMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPEHNP-GNLGGTMRLGIRRTVFKtENSILRKLYGDvPFIEERHR 479
Cdd:TIGR00337 381 GMQLAVIEFARNVAGLEGANSTEFDPDTKYPVVDLLPEQKDiSDLGGTMRLGLYPCILK-PGTLAFKLYGK-EEVYERHR 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28559083   480 HRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLA 546
Cdd:TIGR00337 459 HRYEVNNEYREQIENKGLIVSGTSPDGRLVEIIELPDHPFFVACQFHPEFTSRPNDPHPLFLGFVKA 525
CTP_synth_N pfam06418
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ...
 2-272 0e+00

CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position.


Pssm-ID: 461903  Cd Length: 265  Bit Score: 554.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083     2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:pfam06418   1 KYIFVTGGVVSGLGKGITAASLGRLLKSRGLKVTIIKIDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFLDIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083    82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKvpvdgnKEEPQICVIELGGTIGDIEGMPFVE 161
Cdd:pfam06418  81 LTKDNNITTGKIYQSVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAK------EVGPDVVIVEIGGTVGDIESLPFLE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   162 AFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:pfam06418 155 AIRQLRLEVGRENVLFIHVTLVPYLKAAGELKTKPTQHSVKELRSIGIQPDIIVCRSERPLDEEVKEKIALFCNVPKEAV 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 28559083   242 ICIHDVSSTYRVPVLLEEQSIVKYFKERLHL 272
Cdd:pfam06418 235 ISAPDVSSIYEVPLLLEEQGLDDIILKRLNL 265
CTPS_N cd03113
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ...
 2-268 0e+00

N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product.


Pssm-ID: 349767  Cd Length: 261  Bit Score: 532.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   2 KYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDIN 81
Cdd:cd03113   1 KYIFVTGGVVSGLGKGITASSIGRLLKSRGLRVTAIKIDPYLNVDAGTMSPYEHGEVFVLDDGGETDLDLGNYERFLDVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  82 LYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKVPvdgnkeEPQICVIELGGTIGDIEGMPFVE 161
Cdd:cd03113  81 LTRDNNITTGKIYSEVIEKERRGDYLGKTVQVIPHITDEIKERIRRVAKIP------EPDVCIVEIGGTVGDIESLPFLE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 162 AFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQV 241
Cdd:cd03113 155 ALRQFQFEVGRENFLFIHVTLVPYLEATGEQKTKPTQHSVKELRSLGIQPDIIVCRSEKPLDEETKEKIALFCNVPPEAV 234

                       250       260
                ....*....|....*....|....*..
gi 28559083 242 ICIHDVSSTYRVPVLLEEQSIVKYFKE 268
Cdd:cd03113 235 ISVHDVSSIYEVPLLLEKQGLDDYILR 261
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 299-544 1.53e-128

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 376.12  E-value: 1.53e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 299 CSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITetedpvkfheAWQKLCKADGILVPGGFGIRGT 378
Cdd:cd01746   1 VRIALVGKYVELPDAYLSVLEALKHAGIALGVKLEIKWIDSEDLEEEN----------AEEALKGADGILVPGGFGIRGV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 379 LGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPE-HNPGNLGGTMRLGIRRTVF 457
Cdd:cd01746  71 EGKILAIKYARENNIPFLGICLGMQLAVIEFARNVLGLPDANSTEFDPDTPHPVVDLMPEqKGVKDLGGTMRLGAYPVIL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 458 KtENSILRKLYGdVPFIEERHRHRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPS 537
Cdd:cd01746 151 K-PGTLAHKYYG-KDEVEERHRHRYEVNPEYVDELEEAGLRFSGTDPDGGLVEIVELPDHPFFVGTQFHPEFKSRPLKPH 228


                ....*..
gi 28559083 538 PPYLGLL 544
Cdd:cd01746 229 PLFVGFV 235
GATase pfam00117
Glutamine amidotransferase class-I;
310-546 9.30e-40

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 143.53  E-value: 9.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   310 LRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITEtedpvkfheawqklcKADGILVPGGFGIRGTLG-KLQAISWA 388
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEE---------------NPDGIILSGGPGSPGAAGgAIEAIREA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   389 RTKKIPFLGVCLGMQLAVIEFARNCLNLKDadstefrpnapvplvidmpehnPGNLGGTMRLGIRRTvfktensilRKLY 468
Cdd:pfam00117  67 RELKIPILGICLGHQLLALAFGGKVVKAKK----------------------FGHHGKNSPVGDDGC---------GLFY 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28559083   469 GDVPFIEERHRHRFEVNPNlikqFEQNDLSFVGQDVDGD-RMEIIELANHpyFVGVQFHPEFSSRPMKPSPPYLGLLLA 546
Cdd:pfam00117 116 GLPNVFIVRRYHSYAVDPD----TLPDGLEVTATSENDGtIMGIRHKKLP--IFGVQFHPESILTPHGPEILFNFFIKA 188
PRK06186 PRK06186
hypothetical protein; Validated
 301-547 1.83e-32

hypothetical protein; Validated


Pssm-ID: 180452 [Multi-domain]  Cd Length: 229  Bit Score: 124.69  E-value: 1.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  301 IALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSidlEKITETEDPVKFHEAWqklckadgiLVPGGfGIRGTLG 380
Cdd:PRK06186   4 IALVGDYNPDVTAHQAIPLALDLAAAVLGLPVDYEWLPT---PEITDPEDLAGFDGIW---------CVPGS-PYRNDDG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  381 KLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDADSTEFRPNAP----VPLVIDMPEHNpgnlgGTMRLgirrtv 456
Cdd:PRK06186  71 ALTAIRFARENGIPFLGTCGGFQHALLEYARNVLGWADAAHAETDPEGDrpviAPLSCSLVEKT-----GDIRL------ 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  457 fkTENSILRKLYGdVPFIEERHRHRFEVNPNLIKQFEQNDLSFVGQDVDGDrMEIIELANHPYFVGVQFHPEFSSRPMKP 536
Cdd:PRK06186 140 --RPGSLIARAYG-TLEIEEGYHCRYGVNPEFVAALESGDLRVTGWDEDGD-VRAVELPGHPFFVATLFQPERAALAGRP 215

                        250
                 ....*....|.
gi 28559083  537 SPPYLGLLLAA 547
Cdd:PRK06186 216 PPLVRAFLRAA 226
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 365-529 8.85e-10

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 59.03  E-value: 8.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 365 DGILVPGG-------FG--IRGTLGK---------LQAISWARTKKIPFLGVCLGMQLaviefarncLNlkdadstefrp 426
Cdd:COG2071  51 DGLVLTGGadvdpalYGeePHPELGPidperdafeLALIRAALERGKPVLGICRGMQL---------LN----------- 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 427 napV----PLVIDMPEHNPGNLG---GTMRLGIRRTVFKTENSILRKLYGdvpfieerhRHRFEVNpnlikqfeqndlSF 499
Cdd:COG2071 111 ---ValggTLYQDLPDQVPGALDhrqPAPRYAPRHTVEIEPGSRLARILG---------EEEIRVN------------SL 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 28559083 500 VGQDVD--GDRMEI-----------IELANHPYFVGVQFHPEF 529
Cdd:COG2071 167 HHQAVKrlGPGLRVsarapdgvieaIESPGAPFVLGVQWHPEW 209
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 301-407 1.13e-09

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 56.07  E-value: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 301 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEKITETEDPVkfhEAWQKLCKADGILVPGGFGIRGTL- 379
Cdd:cd01653   1 VAVLLFPGFEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63

                        90       100       110
                ....*....|....*....|....*....|.
gi 28559083 380 ---GKLQAISWARTKKIPFLGVCLGMQLAVI 407
Cdd:cd01653  64 rdeALLALLREAAAAGKPILGICLGAQLLVL 94
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 301-404 3.69e-08

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 51.05  E-value: 3.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 301 IALVGKYTKLRDCYASVFKALEHSAlainhklnlmyidsIDLEKITETEDPVkfhEAWQKLCKADGILVPGGFGIRGTL- 379
Cdd:cd03128   1 VAVLLFGGSEELELASPLDALREAG--------------AEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLa 63

                        90       100
                ....*....|....*....|....*...
gi 28559083 380 ---GKLQAISWARTKKIPFLGVCLGMQL 404
Cdd:cd03128  64 wdeALLALLREAAAAGKPVLGICLGAQL 91
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 392-528 1.19e-06

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 49.56  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083   392 KIPFLGVCLGMQLAVIEFARNcLNLKdadstefrpnapvplvIDMPEHNPGNLGGTMRL--GIRRTVFKTENSILRKLYG 469
Cdd:pfam07722 105 GKPILGICRGFQLLNVALGGT-LYQD----------------IQEQPGFTDHREHCQVApyAPSHAVNVEPGSLLASLLG 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28559083   470 DvPFIEERHRHRF---EVNPNLIkqfeqndlsFVGQDVDGdRMEIIELANHPYFV-GVQFHPE 528
Cdd:pfam07722 168 S-EEFRVNSLHHQaidRLAPGLR---------VEAVAPDG-TIEAIESPNAKGFAlGVQWHPE 219
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 348-431 3.36e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 47.94  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  348 TEDPvkfheawQKLCKADGILVPG----GFGIRG--TLGKLQAISWARTKKIPFLGVCLGMQLavieFAR-------NCL 414
Cdd:PRK13181  29 SSDP-------EEIAGADKVILPGvgafGQAMRSlrESGLDEALKEHVEKKQPVLGICLGMQL----LFEsseegnvKGL 97

                         90
                 ....*....|....*...
gi 28559083  415 NLKDADSTEFRPN-APVP 431
Cdd:PRK13181  98 GLIPGDVKRFRSEpLKVP 115
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 316-404 1.11e-05

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 46.57  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 316 SVFKALEHsaLAINhklnlmyidsidlekITETEDPvkfheawQKLCKADGILVPG-G-FG-----IRGtLGKLQAISWA 388
Cdd:COG0118  15 SVAKALER--LGAE---------------VVVTSDP-------DEIRAADRLVLPGvGaFGdamenLRE-RGLDEAIREA 69

                        90
                ....*....|....*.
gi 28559083 389 RTKKIPFLGVCLGMQL 404
Cdd:COG0118  70 VAGGKPVLGICLGMQL 85
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 359-528 3.22e-05

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 45.77  E-value: 3.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 359 QKLCKADGILVPGGFGirgtlgKLQAISWARTKKI---------------PFLGVCLGMQLAVIEFARNCLNLKDADSTe 423
Cdd:cd01747  50 KLFKSINGILFPGGAV------DIDTSGYARTAKIiynlalerndagdyfPVWGTCLGFELLTYLTSGETLLLEATEAT- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 424 frpNAPVPLvidmpEHNPGNLGGTMrlgirrtvFKT-ENSILRKLyGDVPFIEerHRHRFEVNPnliKQFEQNDL--SF- 499
Cdd:cd01747 123 ---NSALPL-----NFTEDALQSRL--------FKRfPPDLLKSL-ATEPLTM--NNHRYGISP---ENFTENGLlsDFf 180

                       170       180       190
                ....*....|....*....|....*....|....
gi 28559083 500 --VGQDVDGDRMEIIELANH---PYFvGVQFHPE 528
Cdd:cd01747 181 nvLTTNDDWNGVEFISTVEAykyPIY-GVQWHPE 213
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 2-66 3.60e-05

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 43.19  E-value: 3.60e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28559083   2 KYILVTGGViSGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAG--------------TFSPYEHGEVFVLNDGGE 66
Cdd:cd01983   1 RVIAVTGGK-GGVGKTTLAAALAVALAAKGYKVLLIDLDDYVLIDGGggletglllgtivaLLALKKADEVIVVVDPEL 78
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 315-404 1.05e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 43.58  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  315 ASVFKALEHsaLAINHKLnlmyidsidlekiteTEDPvkfheawQKLCKADGILVPG--GFG-----IRGTlGKLQAISW 387
Cdd:PRK13141  13 RSVEKALER--LGAEAVI---------------TSDP-------EEILAADGVILPGvgAFPdamanLRER-GLDEVIKE 67

                         90
                 ....*....|....*..
gi 28559083  388 ARTKKIPFLGVCLGMQL 404
Cdd:PRK13141  68 AVASGKPLLGICLGMQL 84
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 316-404 3.08e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 42.46  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083  316 SVFKALEHSALAInhklnlmyidsidleKITETEDPvkfheawQKLCKADGILVPG---------GFGIRGTLGKLQAIS 386
Cdd:PRK13146  16 SAAKALERAGAGA---------------DVVVTADP-------DAVAAADRVVLPGvgafadcmrGLRAVGLGEAVIEAV 73

                         90
                 ....*....|....*...
gi 28559083  387 WARTKkiPFLGVCLGMQL 404
Cdd:PRK13146  74 LAAGR--PFLGICVGMQL 89
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 363-404 3.92e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 41.78  E-value: 3.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 28559083  363 KADGILVPG--GFGIRGT-LGKL-QAISWARTKKIPFLGVCLGMQL 404
Cdd:PRK13143  38 DADGIVLPGvgAFGAAMEnLSPLrDVILEAARSGKPFLGICLGMQL 83
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 315-404 1.12e-03

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 40.56  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28559083 315 ASVFKALEHsaLAINHKLnlmyidsidlekiteTEDPvkfheawQKLCKADGILVPG----GFGIRG--TLGKLQAISWA 388
Cdd:cd01748  12 RSVANALER--LGAEVII---------------TSDP-------EEILSADKLILPGvgafGDAMANlrERGLIEALKEA 67

                        90
                ....*....|....*.
gi 28559083 389 RTKKIPFLGVCLGMQL 404
Cdd:cd01748  68 IASGKPFLGICLGMQL 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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