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Protein

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

Gene

inhA

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Enoyl-ACP reductase of the type II fatty acid syntase (FAS-II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls. Catalyzes the NADH-dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway. Shows preference for long-chain fatty acyl thioester substrates, and can also use 2-trans-enoyl-CoAs as alternative substrates. The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids.By similarity
Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH) (PubMed:12406221). Overexpressed inhA confers INH and ETH resistance to M.bovis (PubMed:12406221). The mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of NAD and binding of the INH-NAD adduct to the active site of InhA (By similarity). Similarly, the ETH-NAD adduct binds InhA (By similarity).By similarity1 Publication

Catalytic activityi

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

Pathwayi: mycolic acid biosynthesis

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei149May act as an intermediate that passes the hydride ion from NADH to the substrateBy similarity1
Binding sitei158SubstrateBy similarity1
Sitei158Transition state stabilizerBy similarity1
Binding sitei165NADBy similarity1
Binding sitei194NAD; via amide nitrogen and carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 21NADBy similarity2
Nucleotide bindingi64 – 65NADBy similarity2
Nucleotide bindingi95 – 96NADBy similarity2

GO - Molecular functioni

GO - Biological processi

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

UniPathwayiUPA00915.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH]By similarity (EC:1.3.1.9By similarity)
Short name:
ENRBy similarity
Short name:
Enoyl-ACP reductaseBy similarity
Alternative name(s):
FAS-II enoyl-ACP reductaseBy similarity
NADH-dependent 2-trans-enoyl-ACP reductaseBy similarity
Gene namesi
Name:inhA1 Publication
Ordered Locus Names:Mb1520
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001419 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000549151 – 269Enoyl-[acyl-carrier-protein] reductase [NADH]Add BLAST269

Interactioni

Subunit structurei

Homodimer. Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP0A5Y7.
SMRiP0A5Y7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK11611.
OMAiSACKREG.

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.

P0A5Y7-1 [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:March 15, 2005 - v1
Checksum:iF161D6D6A631CA08
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti94S → A in strain: NZ; INH-resistant. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41388 Genomic DNA. Translation: AAB60183.1.
BX248333 Genomic DNA. Translation: CDO42768.1.
RefSeqiNP_855172.1. NC_002945.3.
WP_003407553.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO42768; CDO42768; Mb1520.
GeneIDi1092377.
KEGGimbo:Mb1520.
PATRICi18005028. VBIMycBov88188_1661.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41388 Genomic DNA. Translation: AAB60183.1.
BX248333 Genomic DNA. Translation: CDO42768.1.
RefSeqiNP_855172.1. NC_002945.3.
WP_003407553.1. NC_002945.3.

3D structure databases

ProteinModelPortaliP0A5Y7.
SMRiP0A5Y7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO42768; CDO42768; Mb1520.
GeneIDi1092377.
KEGGimbo:Mb1520.
PATRICi18005028. VBIMycBov88188_1661.

Phylogenomic databases

KOiK11611.
OMAiSACKREG.

Enzyme and pathway databases

UniPathwayiUPA00915.

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_MYCBO
AccessioniPrimary (citable) accession number: P0A5Y7
Secondary accession number(s): P46533, X2BIC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 30, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.