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UniProtKB/Swiss-Prot entry P0A546


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DYR_MYCTU
Primary accession number P0A546
Secondary accession number O33305
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on March 15, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 31)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: folA
Synonyms: dfrA
OrderedLocusNames: Rv2763c, MT2833
ORFNames: MTV002.28c
From
Mycobacterium tuberculosis [TaxID: 1773] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
DOI=10.1038/31159; PubMed=9634230 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., 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.M., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.";
Nature 393:537-544(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
DOI=10.1128/JB.184.19.5479-5490.2002; PubMed=12218036 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).
[3]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
DOI=10.1006/jmbi.1999.3328; PubMed=10623528 [NCBI, ExPASy, EBI, Israel, Japan]
Li R., Sirawaraporn R., Chitnumsub P., Sirawaraporn W., Wooden J., Athappilly F., Turley S., Hol W.G.J.;
"Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs.";
J. Mol. Biol. 295:307-323(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX842580; CAA15559.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK47152.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B70881; B70881.
RefSeq NP_217279.1; -.
NP_337338.1; -.
3D structure databases
PDB
1DF7; X-ray; 1.70 A; A=1-159.[ExPASy / RCSB / EBI]
1DG5; X-ray; 2.00 A; A=1-159.[ExPASy / RCSB / EBI]
1DG7; X-ray; 1.80 A; A=1-159.[ExPASy / RCSB / EBI]
1DG8; X-ray; 2.00 A; A=1-159.[ExPASy / RCSB / EBI]
2CIG; X-ray; 1.90 A; A=1-159.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DF7; -.
1DG5; -.
1DG7; -.
1DG8; -.
2CIG; -.
ModBase P0A546.
Organism-specific databases
TubercuList Rv2763c; -.
Ontologies
GO
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006545; Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009165; Biological process: nucleotide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012259; DHFR.
IPR001796; DHFR_reg.
Graphical view of domain structure.
PANTHER PTHR11549:SF1; DHFR; 1.
Pfam PF00186; DHFR_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00070; DHFR.
PROSITE PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 887777; -.
925455; -.
GenomeReviews AE000516_GR; MT2833.
AL123456_GR; Rv2763c.
KEGG mtc:MT2833; -.
mtu:Rv2763c; -.
TIGR MT2833; -.
Phylogenomic databases
HOGENOM P0A546; -.
Other
ProtoNet P0A546.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   159  159     Dihydrofolate reductase. PRO_0000186400
DOMAIN   1   158  158     DHFR. 
STRAND   2     9  8      
STRAND   12    16  5      
HELIX   25    35  11      
STRAND   38    43  6      
HELIX   44    49  6      
HELIX   52    54  3      
STRAND   60    65  6      
STRAND   76    81  6      
HELIX   82    85  4      
STRAND   88    93  6      
HELIX   97   103  7      
HELIX   104   106  3      
STRAND   108   115  8      
STRAND   136   139  4      
STRAND   150   157  8      
Sequence information
Length: 159 AA [This is the length of the unprocessed precursor] Molecular weight: 17640 Da [This is the MW of the unprocessed precursor] CRC64: F17C038F1B773797 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVGLIWAQAT SGVIGRGGDI PWRLPEDQAH FREITMGHTI VMGRRTWDSL PAKVRPLPGR 

        70         80         90        100        110        120 
RNVVLSRQAD FMASGAEVVG SLEEALTSPE TWVIGGGQVY ALALPYATRC EVTEVDIGLP 

       130        140        150 
REAGDALAPV LDETWRGETG EWRFSRSGLR YRLYSYHRS 

P0A546 in FASTA format

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