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UniProtKB/Swiss-Prot entry P0A5Y6


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

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Entry information
Entry name INHA_MYCTU
Primary accession number P0A5Y6
Secondary accession number P46533
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on March 15, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 39)
Name and origin of the protein
Protein name Enoyl-[acyl-carrier-protein] reductase [NADH]
Synonyms EC 1.3.1.9
NADH-dependent enoyl-ACP reductase
Gene name
Name: inhA
OrderedLocusNames: Rv1484, MT1531
ORFNames: MTCY277.05
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 [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=8284673 [NCBI, ExPASy, EBI, Israel, Japan]
Banerjee A., Dubnau E., Quemard A., Balasubramanian V., Um K.S., Wilson T., Collins D., de Lisle G., Jacobs W.R. Jr.;
"inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis.";
Science 263:227-230(1994).
[2]
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).
[3]
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).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=7886450 [NCBI, ExPASy, EBI, Israel, Japan]
Dessen A., Quemard A., Blanchard J.S., Jacobs W.R. Jr., Sacchettini J.C.;
"Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis.";
Science 267:1638-1641(1995).
[5]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
DOI=10.1126/science.279.5347.98; PubMed=9417034 [NCBI, ExPASy, EBI, Israel, Japan]
Rozwarski D.A., Grant G.A., Barton D.H.R., Jacobs W.R. Jr., Sacchettini J.C.;
"Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.";
Science 279:98-102(1998).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE.
DOI=10.1074/jbc.274.22.15582; PubMed=10336454 [NCBI, ExPASy, EBI, Israel, Japan]
Rozwarski D.A., Vilcheze C., Sugantino M., Bittman R., Sacchettini J.C.;
"Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate.";
J. Biol. Chem. 274:15582-15589(1999).
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
U02492; AAC43210.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX842576; CAB02034.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000516; AAK45796.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G70710; G70710.
RefSeq NP_216000.1; -.
NP_335982.1; -.
3D structure databases
PDB
1BVR; X-ray; 2.80 A; A/B/C/D/E/F=2-269.[ExPASy / RCSB / EBI]
1ENY; X-ray; 2.20 A; A=3-269.[ExPASy / RCSB / EBI]
1ENZ; X-ray; 2.70 A; A=3-269.[ExPASy / RCSB / EBI]
1P44; X-ray; 2.70 A; A/B/C/D/E/F=1-269.[ExPASy / RCSB / EBI]
1P45; X-ray; 2.60 A; A/B=1-269.[ExPASy / RCSB / EBI]
1ZID; X-ray; 2.70 A; A=3-269.[ExPASy / RCSB / EBI]
2AQ8; X-ray; 1.92 A; A=1-269.[ExPASy / RCSB / EBI]
2AQH; X-ray; 2.01 A; A=1-269.[ExPASy / RCSB / EBI]
2AQI; X-ray; 2.20 A; A=1-269.[ExPASy / RCSB / EBI]
2AQK; X-ray; 2.30 A; A=1-269.[ExPASy / RCSB / EBI]
2B35; X-ray; 2.30 A; A/B/C/D/E/F=1-269.[ExPASy / RCSB / EBI]
2B36; X-ray; 2.80 A; A/B/C/D/E/F=1-269.[ExPASy / RCSB / EBI]
2B37; X-ray; 2.60 A; A/B/C/D/E/F=1-269.[ExPASy / RCSB / EBI]
2H7I; X-ray; 1.62 A; A=1-269.[ExPASy / RCSB / EBI]
2H7L; X-ray; 1.73 A; A=1-269.[ExPASy / RCSB / EBI]
2H7M; X-ray; 1.62 A; A=1-269.[ExPASy / RCSB / EBI]
2H7N; X-ray; 1.90 A; A=1-269.[ExPASy / RCSB / EBI]
2H7P; X-ray; 1.86 A; A=1-269.[ExPASy / RCSB / EBI]
2H9I; X-ray; 2.20 A; A=3-269.[ExPASy / RCSB / EBI]
2IDZ; X-ray; 2.00 A; A=2-269.[ExPASy / RCSB / EBI]
2IE0; X-ray; 2.20 A; A=2-269.[ExPASy / RCSB / EBI]
2IEB; X-ray; 2.20 A; A=2-269.[ExPASy / RCSB / EBI]
2IED; X-ray; 2.14 A; A/B/C/D=2-269.[ExPASy / RCSB / EBI]
2NSD; X-ray; 1.90 A; A/B=1-269.[ExPASy / RCSB / EBI]
2NTJ; X-ray; 2.50 A; A/B=3-269.[ExPASy / RCSB / EBI]
2NV6; X-ray; 1.90 A; A=3-269.[ExPASy / RCSB / EBI]
2PR2; X-ray; 2.50 A; A=1-269.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BVR; -.
1ENY; -.
1ENZ; -.
1P44; -.
1P45; -.
1ZID; -.
2AQ8; -.
2AQH; -.
2AQI; -.
2AQK; -.
2B35; -.
2B36; -.
2B37; -.
2H7I; -.
2H7L; -.
2H7M; -.
2H7N; -.
2H7P; -.
2H9I; -.
2IDZ; -.
2IE0; -.
2IEB; -.
2IED; -.
2NSD; -.
2NTJ; -.
2NV6; -.
2PR2; -.
ModBase P0A5Y6.
Organism-specific databases
TubercuList Rv1484; -.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004318; Molecular function: enoyl-[acyl-carrier-protein] reductase (NADH) activity (inferred from electronic annotation from InterPro).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0046677; Biological process: response to antibiotic (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR014358; Enoyl-ACP_rdct.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
PTHR19410:SF12; Enoyl-ACP_rdct; 1.
Genome annotation databases
GeneID 886523; -.
924440; -.
GenomeReviews AE000516_GR; MT1531.
AL123456_GR; Rv1484.
KEGG mtc:MT1531; -.
mtu:Rv1484; -.
TIGR MT1531; -.
Phylogenomic databases
HOGENOM P0A5Y6; -.
Other
BindingDB P0A5Y6; -.
DrugBank DB00609; Ethionamide.
DB00951; Isoniazid.
LinkHub P0A5Y6; -.
ProtoNet P0A5Y6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antibiotic resistance; Complete proteome; Fatty acid biosynthesis; Lipid synthesis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   269  269     Enoyl-[acyl-carrier-protein] reductase [NADH]. PRO_0000054916
NP_BIND   136   165  30     NAD (Potential). 
BINDING   158   158        Substrate. 
VARIANT   94    94  1     S -> A (in strain: NZ; INH-resistant). 
TURN   4     7  4      
STRAND   9    13  5      
HELIX   21    31  11      
STRAND   35    40  6      
HELIX   44    51  8      
STRAND   54    56  3      
STRAND   60    62  3      
HELIX   68    72  5      
HELIX   74    82  9      
STRAND   88    93  6      
HELIX   100   102  3      
STRAND   104   106  3      
HELIX   108   110  3      
HELIX   113   123  11      
HELIX   125   134  10      
HELIX   135   137  3      
STRAND   138   148  11      
STRAND   152   154  3      
HELIX   159   180  22      
TURN   181   183  3      
STRAND   185   191  7      
HELIX   197   203  7      
TURN   204   207  4      
HELIX   209   225  17      
HELIX   236   246  11      
STRAND   255   261  7      
HELIX   264   266  3      
Sequence information
Length: 269 AA [This is the length of the unprocessed precursor] Molecular weight: 28528 Da [This is the MW of the unprocessed precursor] CRC64: F161D6D6A631CA08 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTGLLDGKRI LVSGIITDSS IAFHIARVAQ EQGAQLVLTG FDRLRLIQRI TDRLPAKAPL 

        70         80         90        100        110        120 
LELDVQNEEH LASLAGRVTE AIGAGNKLDG VVHSIGFMPQ TGMGINPFFD APYADVSKGI 

       130        140        150        160        170        180 
HISAYSYASM AKALLPIMNP GGSIVGMDFD PSRAMPAYNW MTVAKSALES VNRFVAREAG 

       190        200        210        220        230        240 
KYGVRSNLVA AGPIRTLAMS AIVGGALGEE AGAQIQLLEE GWDQRAPIGW NMKDATPVAK 

       250        260 
TVCALLSDWL PATTGDIIYA DGGAHTQLL 

P0A5Y6 in FASTA format

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