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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

Organism
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Status
Reviewed-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

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 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 bindingi27ZincUniRule annotation1
Metal bindingi30ZincUniRule annotation1
Metal bindingi46ZincUniRule annotation1
Metal bindingi49ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri27 – 49C4-typeUniRule annotationAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, 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: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:SARI_00533
OrganismiSalmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Taxonomic identifieri41514 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000002084 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003590491 – 304Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST304

Proteomic databases

PRIDEiA9MJ59.

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

STRINGi882884.SARI_00533.

Structurei

3D structure databases

SMRiA9MJ59.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 292CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST270

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri27 – 49C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4107QTG. Bacteria.
COG0777. LUCA.
HOGENOMiHOG000021670.
KOiK01963.
OrthoDBiPOG091H04JK.

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.

A9MJ59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWIERIKSN ITPTRKASIP EGVWTKCDSC GQVLYRAELE RNLEVCPKCD
60 70 80 90 100
HHMRMSARNR LHSLLDEGSL VELGSELEPK DVLKFRDSKK YKDRLASAQK
110 120 130 140 150
ETGEKDALVV MKGTLHGMPV 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 PAPNPDAPRE GVVVPPAPGQ

ESEA
Length:304
Mass (Da):33,172
Last modified:January 20, 2009 - v2
Checksum:iA07B5F851F9B287E
GO

Sequence cautioni

The sequence ABX20459 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000880 Genomic DNA. Translation: ABX20459.1. Different initiation.
RefSeqiWP_000118381.1. NC_010067.1.

Genome annotation databases

EnsemblBacteriaiABX20459; ABX20459; SARI_00533.
KEGGises:SARI_00533.

Similar proteinsi

Entry informationi

Entry nameiACCD_SALAR
AccessioniPrimary (citable) accession number: A9MJ59
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: November 22, 2017
This is version 57 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome