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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Aliivibrio logei (Vibrio logei)
Status
Unreviewed-Annotation score: -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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

[Biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + 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 beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA)
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)DescriptionActionsGraphical viewLength
Metal bindingi29ZincUniRule annotation1
Metal bindingi32ZincUniRule annotation1
Metal bindingi48ZincUniRule annotation1
Metal bindingi51ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 51C4-typeUniRule annotationAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotation
Biological processFatty acid biosynthesisUniRule annotation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-bindingUniRule annotation, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaUniRule annotation (EC:2.1.3.15UniRule annotation)
Short name:
ACCase subunit betaUniRule annotation
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit betaUniRule annotation
Gene namesi
Name:accDUniRule annotation
ORF Names:A6E04_18080Imported
OrganismiAliivibrio logei (Vibrio logei)Imported
Taxonomic identifieri688 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
Proteomesi
  • UP000093523 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

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 annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 294CoA carboxyltransferase N-terminalInterPro annotationAdd BLAST270

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri29 – 51C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-fingerUniRule annotation

Family and domain databases

HAMAPiMF_01395 AcetylCoA_CT_beta, 1 hit
InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR000438 Acetyl_CoA_COase_Trfase_b_su
IPR029045 ClpP/crotonase-like_dom_sf
IPR011762 COA_CT_N
PfamiView protein in Pfam
PF01039 Carboxyl_trans, 1 hit
PRINTSiPR01070 ACCCTRFRASEB
SUPFAMiSSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR00515 accD, 1 hit
PROSITEiView protein in PROSITE
PS50980 COA_CT_NTER, 1 hit

Sequencei

Sequence statusi: Complete.

A0A1B9NU30-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWLEKIFNT SNIVSSRKAS IPEGVWTKCT SCEQVLYSAE LERNLEVCPK
60 70 80 90 100
CDHHMRMKAR KRLETFLDAE GRVELGQEFE PKDLLKFKDS KRYKDRISAA
110 120 130 140 150
QKSSNETDAL IVMQGTLLEL PIVACAFEFS FMGGSMGSVV GARFVKAVDA
160 170 180 190 200
AIENNCPLVC FSASGGARMQ EALMSLMQMA KTSAALARLS RKGLPFFSVL
210 220 230 240 250
TDPTMGGVSA SLAMLGDINI GEPKALIGFA GRRVIEQTVR EDLPEGFQRS
260 270 280 290
EFLLEHGAID MIVDRREMRQ RIGGLMAKMT NQASPLVVPV DGSVKN
Length:296
Mass (Da):32,581
Last modified:November 2, 2016 - v1
Checksum:i75AD21CB8869DC97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
MAJU01000029 Genomic DNA Translation: OCH17540.1
RefSeqiWP_012549831.1, NZ_MAJU01000029.1

Genome annotation databases

EnsemblBacteriaiOCH17540; OCH17540; A6E04_18080

Similar proteinsi

Entry informationi

Entry nameiA0A1B9NU30_ALILO
AccessioniPrimary (citable) accession number: A0A1B9NU30
Entry historyiIntegrated into UniProtKB/TrEMBL: November 2, 2016
Last sequence update: November 2, 2016
Last modified: June 20, 2018
This is version 10 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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