Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha

Gene

accD

Organism
Salinispora arenicola (strain CNS-205)
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 (By similarity).By similarity

Catalytic activityi

[Biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha (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)DescriptionActionsGraphical viewLength
Metal bindingi15ZincBy similarity1
Metal bindingi18ZincBy similarity1
Metal bindingi34ZincBy similarity1
Metal bindingi37ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri15 – 37C4-typeBy similarityAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciSARE391037:G1GA7-2719-MONOMER
UniPathwayiUPA00655; UER00711

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha (EC:2.1.3.15)
Short name:
ACCase subunits beta/alpha
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunits beta/alpha
Gene namesi
Name:accD
Synonyms:accA, accDA
Ordered Locus Names:Sare_2689
OrganismiSalinispora arenicola (strain CNS-205)
Taxonomic identifieri391037 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicromonosporalesMicromonosporaceaeSalinispora
Proteomesi
  • UP000001153 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003899021 – 566Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alphaAdd BLAST566

Proteomic databases

PRIDEiA8M4V8

Interactioni

Subunit structurei

Acetyl-CoA carboxylase is a heterotetramer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits of ACCase subunit beta/alpha.By similarity

Protein-protein interaction databases

STRINGi391037.Sare_2689

Structurei

3D structure databases

ProteinModelPortaliA8M4V8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 280CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST270
Domaini282 – 534CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST253

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 243Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaBy similarityAdd BLAST243
Regioni11 – 534CarboxyltransferasePROSITE-ProRule annotationAdd BLAST524
Regioni244 – 566Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaBy similarityAdd BLAST323

Sequence similaritiesi

In the N-terminal section; belongs to the AccD/PCCB family.Curated
In the C-terminal section; belongs to the AccA family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri15 – 37C4-typeBy similarityAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105D8K Bacteria
COG0777 LUCA
COG0825 LUCA
HOGENOMiHOG000244564
KOiK01962
K01963
OMAiRVLMCAN
OrthoDBiPOG091H04JK

Family and domain databases

HAMAPiMF_00823 AcetylCoA_CT_alpha, 1 hit
MF_01395 AcetylCoA_CT_beta, 1 hit
InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR001095 Acetyl_CoA_COase_a_su
IPR000438 Acetyl_CoA_COase_Trfase_b_su
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
PANTHERiPTHR42853 PTHR42853, 1 hit
PfamiView protein in Pfam
PF03255 ACCA, 1 hit
PF01039 Carboxyl_trans, 1 hit
PRINTSiPR01069 ACCCTRFRASEA
SUPFAMiSSF52096 SSF52096, 2 hits
TIGRFAMsiTIGR00513 accA, 1 hit
PROSITEiView protein in PROSITE
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit

Sequencei

Sequence statusi: Complete.

A8M4V8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPTAPQGGQ LWSRCGGCAS LLYRKRLRRN LDVCPECGAH SRLDASARLA
60 70 80 90 100
QLVDPGSFTA LPDRAPEVDP IGFVDVLPYP HRLTAARSGT GLVEAVVCGT
110 120 130 140 150
ATVAGHRCAI AVMDFRFLGG SLGCAVGELI TRAAERALAD RVPLVVVTAS
160 170 180 190 200
GGARMQEGVL SLMQMATVSQ AIAALRESGV PSISVLTDPT YGGVAASFAT
210 220 230 240 250
NTDVVLAESG ARMGFAGPRV IRQVTGRELP DGFQTAEFLL RHGQVDLVVP
260 270 280 290 300
RHALRGRLAM LLAAAAGGRP PVGGGSRSEY SPGDRPSAAA CRGEGQDAWE
310 320 330 340 350
TVRLARHPGR PTTLDYLETG FDGFVELHGD RLGADCPAVV GGLADLAGRP
360 370 380 390 400
VMVVGHQKGH TTAELMARNF GMASPAGHRK ALRLVRLAAR WGLPVVTLVD
410 420 430 440 450
TPGADPGVDA EEQGQAAAIA ENILTLTTLP TPVVAVITGE GGSGGALALA
460 470 480 490 500
VADRVLMLEH AVYSVISPEG CAAILWPDRS AAPQAARALR LTSADLCRLG
510 520 530 540 550
VVDAVVPEPA PAAHHDPPAA VQAVREAVLA HLVPLLDVPT ATLVRCRRRR
560
FRRFGASRLG VRAGAR
Length:566
Mass (Da):58,920
Last modified:December 4, 2007 - v1
Checksum:i23C9D78B97FE8422
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000850 Genomic DNA Translation: ABV98526.1
RefSeqiWP_012182827.1, NC_009953.1

Genome annotation databases

EnsemblBacteriaiABV98526; ABV98526; Sare_2689
GeneIDi5708363
KEGGisaq:Sare_2689
PATRICifig|391037.6.peg.2724

Similar proteinsi

Entry informationi

Entry nameiACCDA_SALAI
AccessioniPrimary (citable) accession number: A8M4V8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: December 4, 2007
Last modified: June 20, 2018
This is version 76 of the entry and version 1 of the sequence. See 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

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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health