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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic

Gene

accD

Organism
Nandina domestica (Heavenly bamboo)
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 beta, chloroplastic (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 bindingi234ZincUniRule annotation1
Metal bindingi237ZincUniRule annotation1
Metal bindingi253ZincUniRule annotation1
Metal bindingi256ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri234 – 256C4-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 beta, chloroplasticUniRule 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
Encoded oniPlastid; Chloroplast
OrganismiNandina domestica (Heavenly bamboo)
Taxonomic identifieri41776 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesBerberidaceaeNandinoideaeNandina

Subcellular locationi

  • Plastidchloroplast stroma UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003591521 – 497Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST497

Interactioni

Subunit structurei

Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and 2 subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ09FV2.
SMRiQ09FV2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini230 – 497CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST268

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri234 – 256C4-typeUniRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

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.
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.

Q09FV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKEKWWFNS MLFNRELEYR CGLSKSTDGI GPIGNTNGSE DPVIDKNIHC
60 70 80 90 100
WGDSDSSSCN NVDRLFGVRG IRNFISDDTF LVRDSNGDNY SIYFDIENHI
110 120 130 140 150
FEIDNDRYEL ESSFSSYLNS SYLNTGSKSN NHYYDRYMYD TKYSWNNHIN
160 170 180 190 200
SCIDNYLDSE IRINSYFSSG GDNYSKSYIY SYICSESVNS IANASSDIKT
210 220 230 240 250
SANESDSHES DSHMRGKYND LDINKKYRHL WVQCENCYGL NYKKFFRSKF
260 270 280 290 300
NICEQCGYHL KMSSSDRIEL SIDPGTWDPM DDDMVSVDPI EFHSEEEPYK
310 320 330 340 350
DRIDSYQKKT GLTEAVQTGI GQLNGIPIAI GVMDFQFMGG SMGSVVGEKI
360 370 380 390 400
TRLIEYATNR SLPVIIVCAS GGARMQEGSL SLMQMAKISS ASYNYQSNKK
410 420 430 440 450
LLYVSILTSP TTGGVTASFG MLGDIIIAEP NAYIAFAGKR VIEQTLNKIV
460 470 480 490
PDGSQAAEYL FHKGLFDPIV PRNLLKGVLS ELFQLHGFFP VNSNSIK
Length:497
Mass (Da):56,159
Last modified:October 17, 2006 - v1
Checksum:iDBB246D1CA7EFA59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ923117 Genomic DNA. Translation: ABI49872.1.
RefSeqiYP_740659.1. NC_008336.1.

Genome annotation databases

GeneIDi4271605.

Similar proteinsi

Entry informationi

Entry nameiACCD_NANDO
AccessioniPrimary (citable) accession number: Q09FV2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 17, 2006
Last modified: May 10, 2017
This is version 48 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

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