Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - Q62L02 (FABV_BURMA)

Entry version 82 (23 Feb 2022)
Sequence version 1 (25 Oct 2004)
Previous versions | rss
Add a publicationFeedback
Protein

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

Gene

fabV

Organism
Burkholderia mallei (strain ATCC 23344)
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 final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the NADH-dependent reduction of the carbon-carbon double bond in the enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It is also able to reduce trans-2-dodecenoyl-CoA (DD-CoA).

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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Inhibited by triclosan.1 Publication

<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 1728 min(-1) for reductase activity with DD-CoA as substrate (without His tag). kcat is 1242 min(-1) for reductase activity with DD-CoA as substrate (with His tag).1 Publication
  1. KM=2.5 µM for DD-CoA (with His tag)1 Publication
  2. KM=4.4 µM for DD-CoA (without His tag)1 Publication
  3. KM=23 µM for NADH1 Publication

pH dependencei

Optimum pH is 7.9.1 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 NADPHUniRule annotation1
<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 sitei225SubstrateUniRule annotation1
<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 sitei244NADUniRule annotation1 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 bindingi48 – 53NADUniRule annotation6
Nucleotide bindingi74 – 75NADUniRule annotation2
Nucleotide bindingi111 – 112NADUniRule annotation2
Nucleotide bindingi139 – 140NADUniRule annotation2
Nucleotide bindingi273 – 275NADUniRule annotation3

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		BMAL243160:G1G3W-2851-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.3.1.9, 1030

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:
Enoyl-[acyl-carrier-protein] reductase [NADH]1 Publication (EC:1.3.1.91 Publication)
Short name:
ENR1 Publication
Alternative name(s):
NADH-dependent enoyl-ACP reductase1 Publication
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:BMA0885
<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>OrganismiBurkholderia mallei (strain ATCC 23344)
<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 identifieri243160 [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 lineageiBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group ›
<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
  • UP000006693 <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 1

<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%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>Mutagenesisi235Y → A: 250-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi235Y → S: 200-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi244K → A: This mutation causes a small decrease in the affinity for both DD-CoA and NADH, and a 110-fold decrease in catalytic efficiency is observed. Loss of reductase activity; when associated with A-245. 1 Publication1
Mutagenesisi244K → R: This mutation causes a small decrease in the affinity for both DD-CoA and NADH, and a 950-fold decrease in catalytic efficiency is observed. 1 Publication1
Mutagenesisi245K → A: 3-fold decrease in affinity for DD-CoA. Loss of reductase activity; when associated with A-244. 1 Publication1
Mutagenesisi245K → M: 10-fold decrease in affinity for DD-CoA, and 70-fold decrease in catalytic efficiency. 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_00002200381 – 397Enoyl-[acyl-carrier-protein] reductase [NADH]Add BLAST397

<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.

UniRule annotation

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		243160.BMA0885

<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

3D structure databases

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

More...SMRi		Q62L02

Database of comparative protein structure models

More...ModBasei		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_4

Identification of Orthologs from Complete Genome Data

More...OMAi		EGCIEQI

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
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

<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.

Q62L02-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIIKPRVRGF ICVTTHPAGC AASVREQIAY VARRGPIERG PKKVLVIGAS 
        60         70         80         90        100
TGYGLAARIA AAFGVGAATL GVFFERAPAD AKPGTAGWYN SAAFHDEAAA 
       110        120        130        140        150
RGLQATSVNG DAFSDEIKHK TIDAIRRDLG QVDLVVYSVA APRRTHPKTG 
       160        170        180        190        200
VTHQSTLKPI GHAVRLRGID TDNEAIKETL LQPATPDEIA DTVAVMGGED 
       210        220        230        240        250
WRMWIDALDA AGVLADGAKT TAFTYLGEQV THDIYWNGSI GEAKKDLDRT 
       260        270        280        290        300
VLALRGKLAA RGGDARVSVL KAVVTQASSA IPMMPLYLSL LFKVMKARGT 
       310        320        330        340        350
HEGCIEQVDG LLRDSLYSAQ PHVDAEGRLR ADRLELDPAV QARVLELWDQ 
       360        370        380        390 
VTDDNLYTLT DFAGYKAEFL RLFGFGIDGV DYDAPVEPNV RIPNLIE
Length:397
Mass (Da):42,802
Last modified:October 25, 2004 - 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:iD2295F17FDD6D18A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
CP000010 Genomic DNA Translation: AAU49089.1

NCBI Reference Sequences

More...RefSeqi		WP_004192836.1, NC_006348.1
YP_102617.1, NC_006348.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAU49089; AAU49089; BMA0885

Database of genes from NCBI RefSeq genomes

More...GeneIDi		56595374

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bma:BMA0885

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|243160.12.peg.915

<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
CP000010 Genomic DNA Translation: AAU49089.1
RefSeqiWP_004192836.1, NC_006348.1
YP_102617.1, NC_006348.1

3D structure databases

SMRiQ62L02
ModBaseiSearch...

Protein-protein interaction databases

STRINGi243160.BMA0885

Genome annotation databases

EnsemblBacteriaiAAU49089; AAU49089; BMA0885
GeneIDi56595374
KEGGibma:BMA0885
PATRICifig|243160.12.peg.915

Phylogenomic databases

eggNOGiCOG3007, Bacteria
HOGENOMiCLU_057698_1_0_4
OMAiEGCIEQI

Enzyme and pathway databases

UniPathwayiUPA00094
BioCyciBMAL243160:G1G3W-2851-MONOMER
BRENDAi1.3.1.9, 1030

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
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

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_BURMA
<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: Q62L02
<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 25, 2004
Last modified: February 23, 2022
This is version 82 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again