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Entry version 40 (08 May 2019)
Sequence version 1 (16 Apr 2014)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
  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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei149May act as an intermediate that passes the hydride ion from NADH to the substrate1 Publication1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi20 – 21NADCombined sources3 Publications2
Nucleotide bindingi64 – 65NADCombined sources3 Publications2
Nucleotide bindingi95 – 96NADCombined sources3 Publications2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processAntibiotic resistance, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:G185E-5668-MONOMER
MTBH37RV:G185E-5668-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00915

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000000967

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:inhA1 Publication
Ordered Locus Names:Rv1484
ORF Names:MTCY277.05
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83332 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

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TubercuListi
Rv1484

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1849

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000549161 – 269Enoyl-[acyl-carrier-protein] reductase [NADH]Add BLAST269

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei266Phosphothreonine2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P9WGR1

PRoteomics IDEntifications database

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PRIDEi
P9WGR1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P9WGR1

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Protein-protein interaction databases

STRING: functional protein association networks

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STRINGi
83332.Rv1484

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P9WGR1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
5G0SX-ray1.74A/B/C/D1-269[»]
5G0TX-ray1.54A/B/C/D1-269[»]
5G0UX-ray1.73A/B/C/D1-269[»]
5G0VX-ray1.79A/B/C/D1-269[»]
5G0WX-ray1.79A/B/C/D1-269[»]
5JFOX-ray2.91A/B/C/D1-269[»]
5MTPX-ray2.00A/B/C/D/E/F/G/H1-269[»]
5MTQX-ray2.60A/B/C/D/E/F/G/H1-269[»]
5MTRX-ray2.00A/B/C/D/E/F/G/H1-269[»]
5OIFX-ray2.03A/B1-269[»]
5OILX-ray2.76A1-269[»]
5OIMX-ray1.91A1-269[»]
5OINX-ray2.82A/B/C/D1-269[»]
5OITX-ray2.58B/D/F/H1-269[»]
5UGSX-ray2.80A/B/C/D/E/G1-269[»]
5UGTX-ray2.60A/B/E/G1-269[»]
5UGUX-ray1.95A1-269[»]
6EP8X-ray1.80A1-269[»]
6GGMX-ray2.73P/Q53-61[»]
6GH1X-ray2.10P/Q/R/Z53-61[»]
6GH4X-ray2.16P/Q/R/Y53-61[»]
6GHNX-ray2.54P/Q53-61[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P9WGR1

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG4105CSJ Bacteria
COG0623 LUCA

KEGG Orthology (KO)

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KOi
K11611

Identification of Orthologs from Complete Genome Data

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OMAi
GILDMIH

Database for complete collections of gene phylogenies

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PhylomeDBi
P9WGR1

Family and domain databases

Conserved Domains Database

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CDDi
cd05372 ENR_SDR, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR014358 Enoyl-ACP_Rdtase_NADH
IPR036291 NAD(P)-bd_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR43159:SF2 PTHR43159:SF2, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000094 Enoyl-ACP_rdct, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51735 SSF51735, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF161D6D6A631CA08
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U02492 Unassigned DNA Translation: AAC43210.1
AY155363 Genomic DNA Translation: AAN75060.1
AL123456 Genomic DNA Translation: CCP44244.1

Protein sequence database of the Protein Information Resource

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PIRi
G70710

NCBI Reference Sequences

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RefSeqi
NP_216000.1, NC_000962.3
WP_003407553.1, NZ_NVQJ01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
CCP44244; CCP44244; Rv1484

Database of genes from NCBI RefSeq genomes

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GeneIDi
886523

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mtu:Rv1484
mtv:RVBD_1484

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_NVQJ01000004.1

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[»]
5G0SX-ray1.74A/B/C/D1-269[»]
5G0TX-ray1.54A/B/C/D1-269[»]
5G0UX-ray1.73A/B/C/D1-269[»]
5G0VX-ray1.79A/B/C/D1-269[»]
5G0WX-ray1.79A/B/C/D1-269[»]
5JFOX-ray2.91A/B/C/D1-269[»]
5MTPX-ray2.00A/B/C/D/E/F/G/H1-269[»]
5MTQX-ray2.60A/B/C/D/E/F/G/H1-269[»]
5MTRX-ray2.00A/B/C/D/E/F/G/H1-269[»]
5OIFX-ray2.03A/B1-269[»]
5OILX-ray2.76A1-269[»]
5OIMX-ray1.91A1-269[»]
5OINX-ray2.82A/B/C/D1-269[»]
5OITX-ray2.58B/D/F/H1-269[»]
5UGSX-ray2.80A/B/C/D/E/G1-269[»]
5UGTX-ray2.60A/B/E/G1-269[»]
5UGUX-ray1.95A1-269[»]
6EP8X-ray1.80A1-269[»]
6GGMX-ray2.73P/Q53-61[»]
6GH1X-ray2.10P/Q/R/Z53-61[»]
6GH4X-ray2.16P/Q/R/Y53-61[»]
6GHNX-ray2.54P/Q53-61[»]
SMRiP9WGR1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1484

Chemistry databases

BindingDBiP9WGR1
ChEMBLiCHEMBL1849
SwissLipidsiSLP:000000967

PTM databases

iPTMnetiP9WGR1

Proteomic databases

PaxDbiP9WGR1
PRIDEiP9WGR1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44244; CCP44244; Rv1484
GeneIDi886523
KEGGimtu:Rv1484
mtv:RVBD_1484

Organism-specific databases

TubercuListiRv1484

Phylogenomic databases

eggNOGiENOG4105CSJ Bacteria
COG0623 LUCA
KOiK11611
OMAiGILDMIH
PhylomeDBiP9WGR1

Enzyme and pathway databases

UniPathwayi
UPA00915

BioCyciMetaCyc:G185E-5668-MONOMER
MTBH37RV:G185E-5668-MONOMER

Family and domain databases

CDDicd05372 ENR_SDR, 1 hit
InterProiView protein in InterPro
IPR014358 Enoyl-ACP_Rdtase_NADH
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR43159:SF2 PTHR43159:SF2, 1 hit
PIRSFiPIRSF000094 Enoyl-ACP_rdct, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiINHA_MYCTU
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P9WGR1
Secondary accession number(s): F2GEM2
, P0A5Y6, P46533, Q540M9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: May 8, 2019
This is version 40 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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