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Entry version 38 (16 Jan 2019)
Sequence version 1 (18 Apr 2012)
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Protein

Caffeyl-CoA reductase-Etf complex subunit CarE

Gene

carE

Organism
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
Status
Reviewed-Annotation score:

Annotation score:4 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

Caffeyl-CoA reductase-Etf complex catalyzes the reduction of caffeyl-CoA to yield hydrocaffeyl-CoA. It couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. The electron transfer flavoprotein (Etf) mediates the electron transfer between the different donors and acceptors. The iron-sulfur cluster may be involved in electron transport, possibly in the intramolecular electron transfer from the Etf protein subunit to the caffeyl-CoA reductase subunit inside the complex. The complex can also reduce 4-coumaroyl-CoA and feruloyl-CoA.1 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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

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 bindingi335 – 363FADBy similarityAdd BLAST29

<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

<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
Ligand4Fe-4S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
AWOO931626:G1H37-1629-MONOMER

<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:
Caffeyl-CoA reductase-Etf complex subunit CarECurated (EC:1.3.1.1081 Publication)
Alternative name(s):
Electron transfer flavoprotein large subunitCurated
Short name:
ETFLSCurated
Electron transfer flavoprotein subunit alpha1 Publication
Short name:
Alpha-ETF1 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:carE1 Publication
Ordered Locus Names:Awo_c15740
<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>OrganismiAcetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
<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 identifieri931626 [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 lineageiBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeAcetobacterium
<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
  • UP000007177 <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

<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

Keywords - Cellular componenti

Cytoplasm

<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_00004356701 – 396Caffeyl-CoA reductase-Etf complex subunit CarEAdd BLAST396

<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

Part of the homotrimeric caffeyl-CoA reductase-Etf complex composed of (R)-2-hydroxyisocaproyl-CoA dehydratase CarC, and the electron transfer flavoprotein (ETF) alpha (CarE) and beta (CarD) subunits.1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
931626.Awo_c15740

<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

1396
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
6FAHX-ray3.13A/E1-396[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
H6LGM8

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

More...
SMRi
H6LGM8

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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

Belongs to the ETF alpha-subunit/FixB family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C10 Bacteria
COG2025 LUCA

KEGG Orthology (KO)

More...
KOi
K22432

Identification of Orthologs from Complete Genome Data

More...
OMAi
VKVCPAQ

Database of Orthologous Groups

More...
OrthoDBi
1400253at2

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01715 ETF_alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.620, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR029035 DHS-like_NAD/FAD-binding_dom
IPR014730 ETF_a/b_N
IPR001308 ETF_a/FixB
IPR033947 ETF_alpha_N
IPR014731 ETF_asu_C
IPR014729 Rossmann-like_a/b/a_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01012 ETF, 1 hit
PF00766 ETF_alpha, 1 hit
PF13237 Fer4_10, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000089 Electra_flavoP_a, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00893 ETF, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52467 SSF52467, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00198 4FE4S_FER_1, 2 hits
PS51379 4FE4S_FER_2, 2 hits

<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.

H6LGM8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAIKVIEEKC IGCSKCQKSC PFDAITIENK IAVIGDACTN CGTCIDVCPT
60 70 80 90 100
EAILQEGTEK IVRDLSMYKG VWVFAEQREG KIMPVVFELL GEGKKLANEI
110 120 130 140 150
GTELCAILCG SNVAELTDEL FAYGADKVYL ADAPELEKYT TDGYSKIINE
160 170 180 190 200
AIGLYKPEIV LYGATHIGRD LAPCLAVKVN TGLTADCTKL EIDPDDKKIR
210 220 230 240 250
QTRPAFGGNL MATIVCPGSR PQMSTVRPGV MDKAAYDPSQ KGEVIKLDAT
260 270 280 290 300
FNEGDIRTKV LEIVKTTTDN ISISDADFIV SGGMGLGKPE GFELLKQLAD
310 320 330 340 350
KLGGTVATSR ACVDAGWADH AQQVGQTGTT VKPQIYFACG ISGAIQHIAG
360 370 380 390
MQDSDIIIAI NKNENAPIFE VADYGIVGDL YKVIPAIIEE LDKIGK
Length:396
Mass (Da):42,488
Last modified:April 18, 2012 - 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:iDA3AC9778ADAB1AF
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP002987 Genomic DNA Translation: AFA48356.1

NCBI Reference Sequences

More...
RefSeqi
WP_014355959.1, NC_016894.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AFA48356; AFA48356; Awo_c15740

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
awo:Awo_c15740

<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
CP002987 Genomic DNA Translation: AFA48356.1
RefSeqiWP_014355959.1, NC_016894.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6FAHX-ray3.13A/E1-396[»]
ProteinModelPortaliH6LGM8
SMRiH6LGM8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi931626.Awo_c15740

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFA48356; AFA48356; Awo_c15740
KEGGiawo:Awo_c15740

Phylogenomic databases

eggNOGiENOG4105C10 Bacteria
COG2025 LUCA
KOiK22432
OMAiVKVCPAQ
OrthoDBi1400253at2

Enzyme and pathway databases

BioCyciAWOO931626:G1H37-1629-MONOMER

Family and domain databases

CDDicd01715 ETF_alpha, 1 hit
Gene3Di3.40.50.620, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR029035 DHS-like_NAD/FAD-binding_dom
IPR014730 ETF_a/b_N
IPR001308 ETF_a/FixB
IPR033947 ETF_alpha_N
IPR014731 ETF_asu_C
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF01012 ETF, 1 hit
PF00766 ETF_alpha, 1 hit
PF13237 Fer4_10, 1 hit
PIRSFiPIRSF000089 Electra_flavoP_a, 1 hit
SMARTiView protein in SMART
SM00893 ETF, 1 hit
SUPFAMiSSF52467 SSF52467, 1 hit
PROSITEiView protein in PROSITE
PS00198 4FE4S_FER_1, 2 hits
PS51379 4FE4S_FER_2, 2 hits

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 nameiCARE_ACEWD
<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: H6LGM8
<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: March 16, 2016
Last sequence update: April 18, 2012
Last modified: January 16, 2019
This is version 38 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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