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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

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 (PubMed:25227413). 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 (PubMed:7599116). Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates (PubMed:7599116). 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 (PubMed:25227413).1 Publication1 Publication
Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH) (PubMed:8284673, PubMed:12406221, PubMed:16906155, PubMed:17227913). Overexpressed inhA confers INH and ETH resistance to M.tuberculosis (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 (PubMed:9417034, PubMed:16906155). Similarly, the ETH-NAD adduct binds InhA (PubMed:17227913).1 Publication4 Publications

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.5 Publications

Enzyme regulationi

InhA activity is controlled via phosphorylation: phosphorylation on Thr-266 decreases InhA activity (5-fold reduction) and likely negatively regulates biosynthesis of mycolic acids and growth of the bacterium (PubMed:20864541, PubMed:21143326). The antitubercular pro-drug isoniazid (INH) is oxidatively activated by the catalase-peroxidase KatG and then covalently binds NAD to form an adduct that inhibits the activity of InhA (Ref. 5, PubMed:14623976, PubMed:9417034). The inhibitory adduct is the isonicotinic-acyl-NADH where the isonicotinic-acyl group replaces the 4S (and not the 4R) hydrogen of NADH (PubMed:9417034). Similarly, the antitubercular pro-drugs ethionamide (ETH) and prothionamide (PTH) are activated by the flavoprotein monooxygenase EthA, and forms an adduct with NAD (ETH-NAD and PTH-NAD, respectively) that is a tight-binding inhibitor of InhA (PubMed:17227913). Is inhibited by triclosan and derivatives, pyrazole derivative Genz-8575, indole-5-amide Genz-10850, alkyl diphenyl ethers, pyrrolidine carboxamides, arylamides, pyridomycin, methyl-thiazoles, 4-hydroxy-2-pyridones, and N-benzyl-4-((heteroaryl)methyl)benzamides (PubMed:12606558, PubMed:17163639, PubMed:17034137, PubMed:17723305, PubMed:19130456, PubMed:20200152, PubMed:22987724, PubMed:24107081, PubMed:24616444, PubMed:25568071). Pyridomycin shows a unique mode of InhA inhibition by simultaneously blocking parts of the NADH and the lipid substrate-binding pocket of InhA (PubMed:24292073). Is also inhibited by thiadiazole compounds, that have very attractive antitubercular properties (PubMed:27428438).1 Publication18 Publications

Kineticsi

kcat is 320.4 min(-1) for the reduction of 2-trans-dodecenoyl-CoA (at pH 7.5 and 25 degrees Celsius) (PubMed:21143326). kcat is 278 min(-1) for the reduction of 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius) (PubMed:10521269).2 Publications

Manual assertion based on experiment ini

  1. KM=2.0 µM for 2-trans-octenoyl-ACP (at pH 6.8 and 25 degrees Celsius)1 Publication
  2. KM=8.1 µM for NADH (at pH 6.8 and 25 degrees Celsius)1 Publication
  3. KM=66 µM for NADH (at pH 6.8 and 25 degrees Celsius)1 Publication
  4. KM=19.1 µM for NADH (at pH 6.8)1 Publication
  5. KM=13.5 µM for NADH (at pH 6.8 and 25 degrees Celsius)1 Publication
  6. KM=467 µM for 2-trans-octenoyl-CoA (at pH 6.8 and 25 degrees Celsius)1 Publication
  7. KM=528 µM for 2-trans-octenoyl-CoA (at pH 6.8)1 Publication
  8. KM=48 µM for 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)1 Publication
  9. KM=27 µM for 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)1 Publication
  10. KM=40.9 µM for 2-trans-dodecenoyl-CoA (at pH 7.5 and 25 degrees Celsius)1 Publication
  11. KM=1.5 µM for 2-trans-hexadecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)1 Publication
  1. Vmax=2.2 µmol/min/mg enzyme for the reduction of 2-trans-octenoyl-ACP (at pH 6.8 and 25 degrees Celsius)1 Publication
  2. Vmax=3.6 µmol/min/mg enzyme for the reduction of 2-trans-octenoyl-CoA (at pH 6.8 and 25 degrees Celsius)1 Publication
  3. Vmax=0.52 µmol/min/mg enzyme for the reduction of 2-trans-octenoyl-CoA (at pH 6.8 and 25 degrees Celsius)1 Publication
  4. Vmax=15.3 µmol/min/mg enzyme for the reduction of 2-trans-octenoyl-CoA (at pH 6.8)1 Publication
  5. Vmax=5.8 µmol/min/mg enzyme for the reduction of 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)1 Publication
  6. Vmax=11.4 µmol/min/mg enzyme for the reduction of 2-trans-dodecenoyl-CoA (at pH 7.5 and 25 degrees Celsius)1 Publication
  7. Vmax=4.5 µmol/min/mg enzyme for the reduction of 2-trans-hexadecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)1 Publication

Pathwayi: mycolic acid biosynthesis

This protein is involved in the pathway mycolic acid biosynthesis, which is part of Lipid metabolism.1 Publication
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 substrate1 Publication1
Binding sitei158Substrate1 Publication1
Sitei158Transition state stabilizer1 Publication1
Binding sitei165NADCombined sources3 Publications1
Binding sitei194NAD; via amide nitrogen and carbonyl oxygenCombined sources3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 21NADCombined sources3 Publications2
Nucleotide bindingi64 – 65NADCombined sources3 Publications2
Nucleotide bindingi95 – 96NADCombined sources3 Publications2

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

BioCyciMTBH37RV:G185E-5668-MONOMER.
UniPathwayiUPA00915.

Chemistry databases

SwissLipidsiSLP:000000967.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH]1 Publication (EC:1.3.1.95 Publications)
Short name:
ENR1 Publication
Short name:
Enoyl-ACP reductase1 Publication
Alternative name(s):
FAS-II enoyl-ACP reductaseCurated
NADH-dependent 2-trans-enoyl-ACP reductase1 Publication
Gene namesi
Name:inhA1 Publication
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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi94S → A: Confers INH and ETH resistance. The mutant is 17 times more resistant to inhibition by the INH-NAD adduct. 5- to 6-fold decrease in affinity for NADH that results from a perturbation in the hydrogen-bonding network that stabilizes NADH binding. Nearly no effect on the velocity of the enzyme. Has no impact on the susceptibility to pyridomycin. 4 Publications1
Mutagenesisi148D → G: Confers pyridomycin resistance. Has no impact on the susceptibility to isoniazid and moxifloxacin. 14-fold decrease in NADH affinity, while no effect on catalytic activity. 1 Publication1
Mutagenesisi158Y → A: 1500-fold decrease in catalytic activity while no effect on lipid substrate affinity. 1 Publication1
Mutagenesisi158Y → F: 24-fold decrease in catalytic activity while no effect on lipid substrate affinity. 1 Publication1
Mutagenesisi158Y → S: No effect on catalytic activity. 1 Publication1
Mutagenesisi165K → A or M: Loss of enzyme's ability to bind NADH. 1 Publication1
Mutagenesisi165K → Q or R: No effect on the enzyme's catalytic ability or on its ability to bind NADH. 1 Publication1
Mutagenesisi266T → A: No effect on catalytic activity. Loss of phosphorylation. Does not alter growth of M.tuberculosis. 1 Publication1
Mutagenesisi266T → D or E: Severely impairs catalytic activity, as a consequence of a reduced binding affinity to NADH. These single point mutations are lethal to M.tuberculosis. These mutants fail to complement growth and mycolic acid defects of an inhA-thermosensitive M.smegmatis strain, in a similar manner to what is observed following isoniazid treatment. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1849.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000549161 – 269Enoyl-[acyl-carrier-protein] reductase [NADH]Add BLAST269

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei266Phosphothreonine2 Publications1

Post-translational modificationi

Is phosphorylated on Thr-266 in vivo. In vitro, can be phosphorylated by multiple Ser/Thr protein kinases (STPK) such as PknA, PknB, PknE, PknH and PknL. Phosphorylation decreases enzymatic activity.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP9WGR1.

Interactioni

Subunit structurei

Homodimer (PubMed:7599116). Homotetramer (PubMed:10336454, PubMed:16647717).3 Publications

Protein-protein interaction databases

STRINGi83332.Rv1484.

Chemistry databases

BindingDBiP9WGR1.

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 7Combined sources4
Beta strandi9 – 13Combined sources5
Beta strandi16 – 20Combined sources5
Helixi21 – 31Combined sources11
Beta strandi35 – 40Combined sources6
Helixi44 – 51Combined sources8
Beta strandi54 – 56Combined sources3
Beta strandi60 – 62Combined sources3
Helixi68 – 82Combined sources15
Beta strandi88 – 93Combined sources6
Helixi100 – 102Combined sources3
Beta strandi103 – 106Combined sources4
Helixi108 – 110Combined sources3
Helixi113 – 123Combined sources11
Helixi125 – 134Combined sources10
Helixi135 – 137Combined sources3
Beta strandi138 – 148Combined sources11
Beta strandi152 – 154Combined sources3
Turni156 – 158Combined sources3
Helixi159 – 180Combined sources22
Turni181 – 183Combined sources3
Beta strandi185 – 191Combined sources7
Helixi197 – 203Combined sources7
Turni204 – 207Combined sources4
Helixi209 – 225Combined sources17
Helixi236 – 246Combined sources11
Beta strandi247 – 249Combined sources3
Beta strandi255 – 261Combined sources7
Helixi264 – 266Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4CODX-ray2.40B/D/F/H1-269[»]
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[»]
4OIMX-ray1.85A1-269[»]
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[»]
5CPFX-ray3.41A/B/C/D1-269[»]
5JFOX-ray2.91A/B/C/D1-269[»]
ProteinModelPortaliP9WGR1.
SMRiP9WGR1.
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

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
PDB 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[»]
4CODX-ray2.40B/D/F/H1-269[»]
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[»]
4OIMX-ray1.85A1-269[»]
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[»]
5CPFX-ray3.41A/B/C/D1-269[»]
5JFOX-ray2.91A/B/C/D1-269[»]
ProteinModelPortaliP9WGR1.
SMRiP9WGR1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1484.

Chemistry databases

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

UniPathwayiUPA00915.
BioCyciMTBH37RV:G185E-5668-MONOMER.

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: November 30, 2016
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a high-confidence drug target.1 Publication
Many isoniazid- and ethionamide-resistant clinical isolates contain mutations within the inhA locus. Resistance to isoniazid and ethionamide can be conferred by the single substitution of alanine for serine 94; this drug resistance seems to be directly related to a perturbation in the hydrogen-bonding network that decreases the binding of NADH and the INH-NAD adduct.1 Publication1 Publication

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.