LOCUS NP_216111 527 aa linear BCT 19-NOV-2008
DEFINITION L-aspartate oxidase [Mycobacterium tuberculosis H37Rv].
ACCESSION NP_216111
VERSION NP_216111.1 GI:15608733
DBSOURCE REFSEQ: accession NC_000962.2
KEYWORDS complete genome.
SOURCE Mycobacterium tuberculosis H37Rv
ORGANISM Mycobacterium tuberculosis H37Rv
Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium
tuberculosis complex.
REFERENCE 1
AUTHORS Camus,J.C., Pryor,M.J., Medigue,C. and Cole,S.T.
TITLE Re-annotation of the genome sequence of Mycobacterium tuberculosis
H37Rv
JOURNAL Microbiology (Reading, Engl.) 148 (Pt 10), 2967-2973 (2002)
PUBMED 12368430
REFERENCE 2 (residues 1 to 527)
AUTHORS Cole,S.T., Brosch,R., Parkhill,J., Garnier,T., Churcher,C.,
Harris,D., Gordon,S.V., Eiglmeier,K., Gas,S., Barry,C.E. III,
Tekaia,F., Badcock,K., Basham,D., Brown,D., Chillingworth,T.,
Connor,R., Davies,R., Devlin,K., Feltwell,T., Gentles,S.,
Hamlin,N., Holroyd,S., Hornsby,T., Jagels,K., Krogh,A., McLean,J.,
Moule,S., Murphy,L., Oliver,K., Osborne,J., Quail,M.A.,
Rajandream,M.A., Rogers,J., Rutter,S., Seeger,K., Skelton,J.,
Squares,R., Squares,S., Sulston,J.E., Taylor,K., Whitehead,S. and
Barrell,B.G.
TITLE Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence
JOURNAL Nature 393 (6685), 537-544 (1998)
PUBMED 9634230
REMARK Erratum:[Nature 1998 Nov 12;396(6707):190]
REFERENCE 3 (residues 1 to 527)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (13-SEP-2001) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from CAB09074.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..527
/organism="Mycobacterium tuberculosis H37Rv"
/strain="H37Rv"
/db_xref="taxon:83332"
Protein 1..527
/product="L-aspartate oxidase"
/EC_number="1.4.3.16"
/function="QUINOLINATE BIOSYNTHESIS. CATALYZES THE
OXIDATION OF L-ASPARTATE TO IMINOASPARTATE WHICH IS
CONDENSED WITH DIHYDROXYACETONE PHOSPHATE TO QUINOLINATE
UNDER THE ACTION OF QUINOLINATE SYNTHASE A [CATALYTIC
ACTIVITY : L-ASPARTATE + H(2)O + O(2) = OXALOACETATE +
NH(3) + H(2)O(2)]"
/calculated_mol_wt=53654
CDS 1..527
/gene="nadB"
/locus_tag="Rv1595"
/coded_by="NC_000962.2:1795805..1797388"
/experiment="experimental evidence, no additional details
recorded"
/note="catalyzes the formation of oxaloacetate from
L-aspartate"
/transl_table=11
/db_xref="GOA:P65499"
/db_xref="UniProtKB/Swiss-Prot:P65499"
/db_xref="GeneID:886285"
ORIGIN
1 magpawrdaa dvvvigtgva glaaalaadr agrsvvvlsk aaqthvtath yaqggiavvl
61 pdnddsvdah vadtlaagag lcdpdavysi vadgyravtd lvgagarlde svpgrwaltr
121 egghsrrriv haggdatgae vqralqdaag mldirtghva lrvlhdgtav tgllvvrpdg
181 cgiisapsvi latgglghly sattnpagst gdgialglwa gvavsdlefi qfhptmlfag
241 raggrrplit eairgegail vdrqgnsita gvhpmgdlap rdvvaaaida rlkatgdpcv
301 yldargiegf asrfptvtas craagidpvr qpipvvpgah yscggivtdv ygqtellgly
361 aagevartgl hganrlasns lleglvvggr agkaaaahaa aagrsratss atwpepisyt
421 aldrgdlqra msrdasmyra aaglhrlcds lsgaqvrdva crrdfedval tlvaqsvtaa
481 alartesrgc hhraeypctv peqarsivvr gaddanavcv qalvavc
//