LOCUS NP_216848 548 aa linear BCT 19-NOV-2008
DEFINITION malate dehydrogenase [Mycobacterium tuberculosis H37Rv].
ACCESSION NP_216848
VERSION NP_216848.2 GI:57116971
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 548)
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 548)
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 CAB02059.
On Jan 5, 2005 this sequence version replaced gi:15609469.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..548
/organism="Mycobacterium tuberculosis H37Rv"
/strain="H37Rv"
/db_xref="taxon:83332"
Protein 1..548
/product="malate dehydrogenase"
/EC_number="1.1.1.38"
/function="CATALIZES THE OXIDATIVE DECARBOXYLATION OF
MALATE INTO PYRUVATE, IMPORTANT FOR A WIDE RANGE OF
METABOLIC PATHWAYS [CATALYTIC ACTIVITY: (S)-MALATE +
NAD(+) = PYRUVATE + CO(2) + NADH]."
/calculated_mol_wt=59292
CDS 1..548
/gene="mez"
/locus_tag="Rv2332"
/coded_by="NC_000962.2:2605108..2606754"
/note="malic enzyme; oxaloacetate-decarboxylating;
NAD-dependent; catalyzes the formation of pyruvate form
malate"
/transl_table=11
/db_xref="GOA:P71880"
/db_xref="UniProtKB/Swiss-Prot:P71880"
/db_xref="GeneID:887962"
ORIGIN
1 msdarvprip aalsapslnr gvgfthaqrr rlgltgrlps avltldqqae rvwhqlqsla
61 telgrnllle qlhyrhevly fkvladhlpe lmpvvytptv geaiqrfsde yrgqrglfls
121 idepdeieea fntlglgped vdlivctdae ailgigdwgv ggiqiavgkl alytagggvd
181 prrclavsld vgtdneqlla dpfylgnrha rrrgreydef vsryietaqr lfprailhfe
241 dfgpanarki ldtygtdycv fnddmqgtga vvlaavysgl kvtgiplrdq tivvfgagta
301 gmgiadqird amvadgatle qavsqiwpid rpgllfddmd dlrdfqvpya knrhqlgvav
361 gdrvglsdai kiasptillg cstvygaftk evveamtasc khpmifplsn ptsrmeaipa
421 dvlawsngra llatgspvap vefdettyvi gqannvlafp giglgvivag arlitrrmlh
481 aaakaiahqa nptnpgdsll pdvqnlrais ttvaeavyra avqdgvasrt hddvrqaivd
541 tmwlpayd
//