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Reviewed, UniProtKB/Swiss-Prot P0A5Y7 (INHA_MYCBO)

Last modified September 2, 2008. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADH]
    EC=1.3.1.9
Alternative name(s):
    NADH-dependent enoyl-ACP reductase
Gene names
Name: inhA
Ordered Locus Names: Mb1520
OrganismMycobacterium bovis [Complete proteome] [HAMAP]
Taxonomic identifier1765 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Involved in the resistance against the antituberculosis drugs isoniazid and ethionamide.

Catalytic activity

Acyl-[acyl-carrier-protein] + NAD(+) = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Context: Mycolic acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Ontologies

Keywords

   Biological processAntibiotic resistance
Fatty acid biosynthesis
Lipid synthesis
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 269269Enoyl-[acyl-carrier-protein] reductase [NADH]

Regions

Nucleotide binding136 – 16530NAD Potential

Sites

Binding site1581Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A5Y7-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: F161D6D6A631CA08

FASTA26928,528
        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 

« Hide

References

« Hide 'large scale' references
[1]"inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis."
Banerjee A., Dubnau E., Quemard A., Balasubramanian V., Um K.S., Wilson T., Collins D., de Lisle G., Jacobs W.R. Jr.
Science 263:227-230(1994) [PubMed: 8284673] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BCG.
[2]"Effect of inhA and katG on isoniazid resistance and virulence of Mycobacterium bovis."
Wilson T.M., de Lisle G.W., Collins D.M.
Mol. Microbiol. 15:1009-1015(1995) [PubMed: 7623658] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: WAG201.
[3]"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. expand/collapse author list , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases

U41388 Genomic DNA. Translation: AAB60183.1.
BX248339 Genomic DNA. Translation: CAD96187.1.
RefSeqNP_855172.1.

3D structure databases

SMRP0A5Y7. Positions 2-269.
ModBaseSearch...

Genome annotation databases

GeneID1092377.
GenomeReviewsGene locus Mb1520 in contig BX248333_GR.
KEGGmbo:Mb1520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0A5Y7.

Family and domain databases

InterProIPR002198. DHase_sc/Rdtase_SDR.
IPR014358. Enoyl-ACP_rdct.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PTHR19410:SF12. Enoyl-ACP_rdct. 1 hit.
ProDomP0A5Y7.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

BindingDBP0A5Y7.
ProtoNetSearch...

Entry information

Entry nameINHA_MYCBO
AccessionPrimary (citable) accession number: P0A5Y7
Secondary accession number(s): P46533
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: September 2, 2008
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents