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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.UniRule annotation

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA), Biotin carboxylase (accC), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271ZincUniRule annotation
Metal bindingi30 – 301ZincUniRule annotation
Metal bindingi46 – 461ZincUniRule annotation
Metal bindingi49 – 491ZincUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri27 – 4923C4-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3153-MONOMER.
ECOO157:ACCD-MONOMER.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaUniRule annotation (EC:6.4.1.2UniRule annotation)
Short name:
ACCase subunit betaUniRule annotation
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit betaUniRule annotation
Gene namesi
Name:accDUniRule annotation
Ordered Locus Names:Z3578, ECs3200
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaPRO_0000199771Add
BLAST

Proteomic databases

PRIDEiP0A9Q6.

Interactioni

Subunit structurei

Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).UniRule annotation

Protein-protein interaction databases

MINTiMINT-1234633.
STRINGi155864.Z3578.

Structurei

3D structure databases

ProteinModelPortaliP0A9Q6.
SMRiP0A9Q6. Positions 23-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri27 – 4923C4-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4108IDZ. Bacteria.
COG0777. LUCA.
HOGENOMiHOG000021670.
KOiK01963.
OMAiPEGLWIK.
OrthoDBiEOG6HQSSF.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_01395. AcetylCoA_CT_beta.
InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSiPR01070. ACCCTRFRASEB.
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR00515. accD. 1 hit.
PROSITEiPS50980. COA_CT_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9Q6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWIERIKSN ITPTRKASIP EGVWTKCDSC GQVLYRAELE RNLEVCPKCD
60 70 80 90 100
HHMRMTARNR LHSLLDEGSL VELGSELEPK DVLKFRDSKK YKDRLASAQK
110 120 130 140 150
ETGEKDALVV MKGTLYGMPV VAAAFEFAFM GGSMGSVVGA RFVRAVEQAL
160 170 180 190 200
EDNCPLICFS ASGGARMQEA LMSLMQMAKT SAALAKMQER GLPYISVLTD
210 220 230 240 250
PTMGGVSASF AMLGDLNIAE PKALIGFAGP RVIEQTVREK LPPGFQRSEF
260 270 280 290 300
LIEKGAIDMI VRRPEMRLKL ASILAKLMNL PAPNPEAPRE GVVVPPVPDQ

EPEA
Length:304
Mass (Da):33,322
Last modified:July 19, 2005 - v1
Checksum:i401FEC94D728F3CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57445.1.
BA000007 Genomic DNA. Translation: BAB36623.1.
PIRiA85873.
H91028.
RefSeqiNP_311227.1. NC_002695.1.
WP_000118404.1. NZ_LPWC01000322.1.

Genome annotation databases

EnsemblBacteriaiAAG57445; AAG57445; Z3578.
BAB36623; BAB36623; BAB36623.
GeneIDi916908.
KEGGiece:Z3578.
ecs:ECs3200.
PATRICi18355790. VBIEscCol44059_3096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57445.1.
BA000007 Genomic DNA. Translation: BAB36623.1.
PIRiA85873.
H91028.
RefSeqiNP_311227.1. NC_002695.1.
WP_000118404.1. NZ_LPWC01000322.1.

3D structure databases

ProteinModelPortaliP0A9Q6.
SMRiP0A9Q6. Positions 23-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1234633.
STRINGi155864.Z3578.

Proteomic databases

PRIDEiP0A9Q6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57445; AAG57445; Z3578.
BAB36623; BAB36623; BAB36623.
GeneIDi916908.
KEGGiece:Z3578.
ecs:ECs3200.
PATRICi18355790. VBIEscCol44059_3096.

Phylogenomic databases

eggNOGiENOG4108IDZ. Bacteria.
COG0777. LUCA.
HOGENOMiHOG000021670.
KOiK01963.
OMAiPEGLWIK.
OrthoDBiEOG6HQSSF.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciECOL386585:GJFA-3153-MONOMER.
ECOO157:ACCD-MONOMER.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_01395. AcetylCoA_CT_beta.
InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSiPR01070. ACCCTRFRASEB.
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR00515. accD. 1 hit.
PROSITEiPS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiACCD_ECO57
AccessioniPrimary (citable) accession number: P0A9Q6
Secondary accession number(s): P08193, P76937, P78251
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 19, 2005
Last modified: May 11, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.