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Protein

Enoyl-[acyl-carrier-protein] reductase [NADH]

Gene

inhA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi136 – 16530NADSequence analysisAdd
BLAST

GO - Molecular functioni

  • enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: MTBBASE
  • fatty acid binding Source: MTBBASE
  • NAD+ binding Source: MTBBASE

GO - Biological processi

  • fatty acid elongation Source: MTBBASE
  • mycolic acid biosynthetic process Source: MTBBASE
  • response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic resistance, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00094.

Chemistry

SwissLipidsiSLP:000000967.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] (EC:1.3.1.9)
Alternative name(s):
NADH-dependent enoyl-ACP reductase
Gene namesi
Name:inhA
Ordered Locus Names:Rv1484
ORF Names:MTCY277.05
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1484.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1849.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Enoyl-[acyl-carrier-protein] reductase [NADH]PRO_0000054916Add
BLAST

Proteomic databases

PaxDbiP9WGR1.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv1484.

Chemistry

BindingDBiP9WGR1.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74Combined sources
Beta strandi9 – 135Combined sources
Beta strandi16 – 205Combined sources
Helixi21 – 3111Combined sources
Beta strandi35 – 406Combined sources
Helixi44 – 518Combined sources
Beta strandi54 – 563Combined sources
Beta strandi60 – 623Combined sources
Helixi68 – 8215Combined sources
Beta strandi88 – 936Combined sources
Helixi100 – 1023Combined sources
Beta strandi103 – 1064Combined sources
Helixi108 – 1103Combined sources
Helixi113 – 12311Combined sources
Helixi125 – 13410Combined sources
Helixi135 – 1373Combined sources
Beta strandi138 – 14811Combined sources
Beta strandi152 – 1543Combined sources
Turni156 – 1583Combined sources
Helixi159 – 18022Combined sources
Turni181 – 1833Combined sources
Beta strandi185 – 1917Combined sources
Helixi197 – 2037Combined sources
Turni204 – 2074Combined sources
Helixi209 – 22517Combined sources
Helixi236 – 24611Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi255 – 2617Combined sources
Helixi264 – 2663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVRX-ray2.80A/B/C/D/E/F2-269[»]
1ENYX-ray2.20A3-269[»]
1ENZX-ray2.70A3-269[»]
1P44X-ray2.70A/B/C/D/E/F1-269[»]
1P45X-ray2.60A/B1-269[»]
1ZIDX-ray2.70A3-269[»]
2AQ8X-ray1.92A1-269[»]
2AQHX-ray2.01A1-269[»]
2AQIX-ray2.20A1-269[»]
2AQKX-ray2.30A1-269[»]
2B35X-ray2.30A/B/C/D/E/F1-269[»]
2B36X-ray2.80A/B/C/D/E/F1-269[»]
2B37X-ray2.60A/B/C/D/E/F1-269[»]
2H9IX-ray2.20A2-269[»]
2IDZX-ray2.00A2-269[»]
2IE0X-ray2.20A2-269[»]
2IEBX-ray2.20A2-269[»]
2IEDX-ray2.14A/B/C/D2-269[»]
2NSDX-ray1.90A/B1-269[»]
2NTJX-ray2.50A/B3-269[»]
2NV6X-ray1.90A3-269[»]
2PR2X-ray2.50A1-269[»]
2X22X-ray2.10A/B1-269[»]
2X23X-ray1.81A/B/E/G1-269[»]
3FNEX-ray1.98A/B/C/D1-269[»]
3FNFX-ray2.30A/B/C/D1-269[»]
3FNGX-ray1.97A1-269[»]
3FNHX-ray2.80A1-269[»]
3OEWX-ray2.20A1-269[»]
3OEYX-ray2.00A1-269[»]
3OF2X-ray2.00A1-269[»]
4BGEX-ray2.25A/B/C/D/E/F1-269[»]
4BGIX-ray2.09A/B/C/D/E/F2-269[»]
4BIIX-ray1.95A/B/C/D1-269[»]
4BQPX-ray1.89A/B/C/D/E/F1-269[»]
4BQRX-ray2.05A/B/C/D1-269[»]
4D0RX-ray2.75A1-269[»]
4D0SX-ray1.64A/B/C/D1-269[»]
4DQUX-ray2.45A1-269[»]
4DREX-ray2.40A1-269[»]
4DTIX-ray1.90A1-269[»]
4OHUX-ray1.60A/B/C/D1-269[»]
4OXKX-ray1.84A/B/C/D1-269[»]
4OXNX-ray2.29A/B1-269[»]
4OXYX-ray2.35A/B/C/D1-269[»]
4OYRX-ray2.30A/B/C/D1-269[»]
4QXMX-ray2.20A/C/E/G1-269[»]
4R9RX-ray2.90A/C/E/G1-269[»]
4R9SX-ray3.20A/C/E/G1-269[»]
4TRJX-ray1.73A1-269[»]
4TRMX-ray1.80A/B/C/D/E/F1-269[»]
4TRNX-ray1.95A1-269[»]
4TROX-ray1.40A1-269[»]
4TZKX-ray1.62A1-269[»]
4TZTX-ray1.86A1-269[»]
4U0JX-ray1.62A1-269[»]
4U0KX-ray1.90A1-269[»]
4UVDX-ray1.82A1-269[»]
4UVEX-ray1.99A1-269[»]
4UVGX-ray1.92A1-269[»]
4UVHX-ray1.89A/B/C/D1-269[»]
4UVIX-ray1.73A/B/C/D1-269[»]
5COQX-ray2.30A/B/C/D1-269[»]
5CP8X-ray2.40A1-269[»]
5CPBX-ray2.00A/B/C/D/E/F1-269[»]
ProteinModelPortaliP9WGR1.
SMRiP9WGR1. Positions 2-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CSJ. Bacteria.
COG0623. LUCA.
KOiK11611.
OMAiSACKREG.
PhylomeDBiP9WGR1.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 1 hit.
PTHR24322:SF317. PTHR24322:SF317. 1 hit.
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WGR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGLLDGKRI LVSGIITDSS IAFHIARVAQ EQGAQLVLTG FDRLRLIQRI
60 70 80 90 100
TDRLPAKAPL LELDVQNEEH LASLAGRVTE AIGAGNKLDG VVHSIGFMPQ
110 120 130 140 150
TGMGINPFFD APYADVSKGI HISAYSYASM AKALLPIMNP GGSIVGMDFD
160 170 180 190 200
PSRAMPAYNW MTVAKSALES VNRFVAREAG KYGVRSNLVA AGPIRTLAMS
210 220 230 240 250
AIVGGALGEE AGAQIQLLEE GWDQRAPIGW NMKDATPVAK TVCALLSDWL
260
PATTGDIIYA DGGAHTQLL
Length:269
Mass (Da):28,528
Last modified:April 16, 2014 - v1
Checksum:iF161D6D6A631CA08
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941S → A in strain: NZ; INH-resistant.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02492 Unassigned DNA. Translation: AAC43210.1.
AY155363 Genomic DNA. Translation: AAN75060.1.
AL123456 Genomic DNA. Translation: CCP44244.1.
PIRiG70710.
RefSeqiNP_216000.1. NC_000962.3.
WP_003407553.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44244; CCP44244; Rv1484.
GeneIDi886523.
KEGGimtu:Rv1484.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02492 Unassigned DNA. Translation: AAC43210.1.
AY155363 Genomic DNA. Translation: AAN75060.1.
AL123456 Genomic DNA. Translation: CCP44244.1.
PIRiG70710.
RefSeqiNP_216000.1. NC_000962.3.
WP_003407553.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVRX-ray2.80A/B/C/D/E/F2-269[»]
1ENYX-ray2.20A3-269[»]
1ENZX-ray2.70A3-269[»]
1P44X-ray2.70A/B/C/D/E/F1-269[»]
1P45X-ray2.60A/B1-269[»]
1ZIDX-ray2.70A3-269[»]
2AQ8X-ray1.92A1-269[»]
2AQHX-ray2.01A1-269[»]
2AQIX-ray2.20A1-269[»]
2AQKX-ray2.30A1-269[»]
2B35X-ray2.30A/B/C/D/E/F1-269[»]
2B36X-ray2.80A/B/C/D/E/F1-269[»]
2B37X-ray2.60A/B/C/D/E/F1-269[»]
2H9IX-ray2.20A2-269[»]
2IDZX-ray2.00A2-269[»]
2IE0X-ray2.20A2-269[»]
2IEBX-ray2.20A2-269[»]
2IEDX-ray2.14A/B/C/D2-269[»]
2NSDX-ray1.90A/B1-269[»]
2NTJX-ray2.50A/B3-269[»]
2NV6X-ray1.90A3-269[»]
2PR2X-ray2.50A1-269[»]
2X22X-ray2.10A/B1-269[»]
2X23X-ray1.81A/B/E/G1-269[»]
3FNEX-ray1.98A/B/C/D1-269[»]
3FNFX-ray2.30A/B/C/D1-269[»]
3FNGX-ray1.97A1-269[»]
3FNHX-ray2.80A1-269[»]
3OEWX-ray2.20A1-269[»]
3OEYX-ray2.00A1-269[»]
3OF2X-ray2.00A1-269[»]
4BGEX-ray2.25A/B/C/D/E/F1-269[»]
4BGIX-ray2.09A/B/C/D/E/F2-269[»]
4BIIX-ray1.95A/B/C/D1-269[»]
4BQPX-ray1.89A/B/C/D/E/F1-269[»]
4BQRX-ray2.05A/B/C/D1-269[»]
4D0RX-ray2.75A1-269[»]
4D0SX-ray1.64A/B/C/D1-269[»]
4DQUX-ray2.45A1-269[»]
4DREX-ray2.40A1-269[»]
4DTIX-ray1.90A1-269[»]
4OHUX-ray1.60A/B/C/D1-269[»]
4OXKX-ray1.84A/B/C/D1-269[»]
4OXNX-ray2.29A/B1-269[»]
4OXYX-ray2.35A/B/C/D1-269[»]
4OYRX-ray2.30A/B/C/D1-269[»]
4QXMX-ray2.20A/C/E/G1-269[»]
4R9RX-ray2.90A/C/E/G1-269[»]
4R9SX-ray3.20A/C/E/G1-269[»]
4TRJX-ray1.73A1-269[»]
4TRMX-ray1.80A/B/C/D/E/F1-269[»]
4TRNX-ray1.95A1-269[»]
4TROX-ray1.40A1-269[»]
4TZKX-ray1.62A1-269[»]
4TZTX-ray1.86A1-269[»]
4U0JX-ray1.62A1-269[»]
4U0KX-ray1.90A1-269[»]
4UVDX-ray1.82A1-269[»]
4UVEX-ray1.99A1-269[»]
4UVGX-ray1.92A1-269[»]
4UVHX-ray1.89A/B/C/D1-269[»]
4UVIX-ray1.73A/B/C/D1-269[»]
5COQX-ray2.30A/B/C/D1-269[»]
5CP8X-ray2.40A1-269[»]
5CPBX-ray2.00A/B/C/D/E/F1-269[»]
ProteinModelPortaliP9WGR1.
SMRiP9WGR1. Positions 2-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1484.

Chemistry

BindingDBiP9WGR1.
ChEMBLiCHEMBL1849.
SwissLipidsiSLP:000000967.

Proteomic databases

PaxDbiP9WGR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44244; CCP44244; Rv1484.
GeneIDi886523.
KEGGimtu:Rv1484.

Organism-specific databases

TubercuListiRv1484.

Phylogenomic databases

eggNOGiENOG4105CSJ. Bacteria.
COG0623. LUCA.
KOiK11611.
OMAiSACKREG.
PhylomeDBiP9WGR1.

Enzyme and pathway databases

UniPathwayiUPA00094.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 1 hit.
PTHR24322:SF317. PTHR24322:SF317. 1 hit.
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiINHA_MYCTU
AccessioniPrimary (citable) accession number: P9WGR1
Secondary accession number(s): F2GEM2
, P0A5Y6, P46533, Q540M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: April 13, 2016
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Target of the preferred antitubercular drug isoniazid (INH) which specifically inhibits InhA by covalent attachment of the activated form of the drug to the nicotinamide ring of nicotinamide adenine dinucleotide bound within the active site of the enzyme. Involved in the resistance against both isoniazid and ethionamide (ETH).
Was identified as a high-confidence drug target.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.