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Entry version 93 (25 May 2022)
Sequence version 1 (01 Oct 2001)
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Protein

Trans-2-enoyl-CoA reductase [NADH]

Gene

fabV

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
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

Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of the carbon-carbon double bond of crotonyl-CoA to yield butyryl-CoA.

1 Publication

Miscellaneous

Possesses high activity for the reduction reaction, but no activity for the reverse oxidation reaction.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 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 28.2 sec(-1) for reductase activity (at pH 6.2 and 25 degrees Celsius).1 Publication
  1. KM=105.4 µM for NAD (at pH 6.2 and 25 degrees Celsius)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.Curated
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)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>Sitei75Plays an important role in discriminating NADH against NADPH1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei225Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei235Proton donorUniRule annotation1 Publication1
Binding sitei244NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi47 – 52NAD1 Publication6
Nucleotide bindingi74 – 75NAD1 Publication2
Nucleotide bindingi111 – 112NAD1 Publication2
Nucleotide bindingi139 – 140NAD1 Publication2
Nucleotide bindingi274 – 276NAD1 Publication3

<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

  • NAD binding Source: UniProtKB
  • trans-2-enoyl-CoA reductase (NAD+) activity Source: UniProtKB

GO - Biological processi

<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 processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNAD

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.1.44, 1452

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

More...
UniPathwayi
UPA00094

<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%5Fand%5Ftaxonomy%5Fsection">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:
Trans-2-enoyl-CoA reductase [NADH]1 Publication (EC:1.3.1.441 Publication)
Short name:
TER1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:fabV1 Publication
Ordered Locus Names:CA_C0462
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri272562 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaFirmicutesClostridiaEubacterialesClostridiaceaeClostridium
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000814 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

<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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Used in the biosynthesis of medium-chain volatile alcohols as biofuels engineered by microorganisms. The switch from the native flavin-dependent enoyl-CoA reductase used in the production of n-butanol, a key second-generation biofuel, to a flavin-independent trans-enoyl-CoA reductase from C.acetobutylicum leads to an order of magnitude increase in product yield in engineered E.coli.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi11F → K: Slight decrease of catalytic efficiency and 3-fold increase of the affinity for NADH compared to wild-type. 1 Publication1
Mutagenesisi75E → A: Able to use both NADH and NADPH as cofactor. 1 Publication1
Mutagenesisi225Y → A: 12-fold decrease of catalytic efficiency and slight decrease of the affinity for NADH compared to wild-type. 1 Publication1
Mutagenesisi235Y → F: Loss of reductase activity. 1 Publication1
Mutagenesisi244K → A: Loss of reductase activity. 1 Publication1
Mutagenesisi245K → A: Slight decrease of catalytic efficiency and affinity for NADH compared to wild-type. 1 Publication1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002200401 – 398Trans-2-enoyl-CoA reductase [NADH]Add BLAST398

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
272562.CA_C0462

<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

1398
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
Q97LU2

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

More...
SMRi
Q97LU2

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

Belongs to the TER reductase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3007, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_057698_1_0_9

Identification of Orthologs from Complete Genome Data

More...
OMAi
EGCIEQI

Database of Orthologous Groups

More...
OrthoDBi
678530at2

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01838, FabV_reductase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR024906, Eno_Rdtase_FAD-bd_dom
IPR024910, Enoyl-CoA_Rdtase_cat_dom
IPR036291, NAD(P)-bd_dom_sf
IPR010758, Trans-2-enoyl-CoA_reductase

The PANTHER Classification System

More...
PANTHERi
PTHR37480, PTHR37480, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07055, Eno-Rase_FAD_bd, 1 hit
PF12242, Eno-Rase_NADH_b, 1 hit
PF12241, Enoyl_reductase, 1 hit

Superfamily database of structural and functional annotation

More...
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q97LU2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIVKAKFVKG FIRDVHPYGC RREVLNQIDY CKKAIGFRGP KKVLIVGASS
60 70 80 90 100
GFGLATRISV AFGGPEAHTI GVSYETGATD RRIGTAGWYN NIFFKEFAKK
110 120 130 140 150
KGLVAKNFIE DAFSNETKDK VIKYIKDEFG KIDLFVYSLA APRRKDYKTG
160 170 180 190 200
NVYTSRIKTI LGDFEGPTID VERDEITLKK VSSASIEEIE ETRKVMGGED
210 220 230 240 250
WQEWCEELLY EDCFSDKATT IAYSYIGSPR TYKIYREGTI GIAKKDLEDK
260 270 280 290 300
AKLINEKLNR VIGGRAFVSV NKALVTKASA YIPTFPLYAA ILYKVMKEKN
310 320 330 340 350
IHENCIMQIE RMFSEKIYSN EKIQFDDKGR LRMDDLELRK DVQDEVDRIW
360 370 380 390
SNITPENFKE LSDYKGYKKE FMNLNGFDLD GVDYSKDLDI ELLRKLEP
Length:398
Mass (Da):45,650
Last modified:October 1, 2001 - 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:i59324A21CA466DFC
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

More...
DDBJi
Links Updated
AE001437 Genomic DNA Translation: AAK78442.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G96956

NCBI Reference Sequences

More...
RefSeqi
NP_347102.1, NC_003030.1
WP_010963784.1, NC_003030.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAK78442; AAK78442; CA_C0462

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
44996971

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cac:CA_C0462

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|272562.8.peg.661

<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
AE001437 Genomic DNA Translation: AAK78442.1
PIRiG96956
RefSeqiNP_347102.1, NC_003030.1
WP_010963784.1, NC_003030.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4EUEX-ray2.00A1-398[»]
4EUFX-ray2.70A1-398[»]
4EUHX-ray2.10A1-398[»]
AlphaFoldDBiQ97LU2
SMRiQ97LU2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi272562.CA_C0462

Genome annotation databases

EnsemblBacteriaiAAK78442; AAK78442; CA_C0462
GeneIDi44996971
KEGGicac:CA_C0462
PATRICifig|272562.8.peg.661

Phylogenomic databases

eggNOGiCOG3007, Bacteria
HOGENOMiCLU_057698_1_0_9
OMAiEGCIEQI
OrthoDBi678530at2

Enzyme and pathway databases

UniPathwayiUPA00094
BRENDAi1.3.1.44, 1452

Family and domain databases

HAMAPiMF_01838, FabV_reductase, 1 hit
InterProiView protein in InterPro
IPR024906, Eno_Rdtase_FAD-bd_dom
IPR024910, Enoyl-CoA_Rdtase_cat_dom
IPR036291, NAD(P)-bd_dom_sf
IPR010758, Trans-2-enoyl-CoA_reductase
PANTHERiPTHR37480, PTHR37480, 1 hit
PfamiView protein in Pfam
PF07055, Eno-Rase_FAD_bd, 1 hit
PF12242, Eno-Rase_NADH_b, 1 hit
PF12241, Enoyl_reductase, 1 hit
SUPFAMiSSF51735, SSF51735, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiFABV_CLOAB
<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: Q97LU2
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2001
Last modified: May 25, 2022
This is version 93 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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