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 subunit beta, chloroplastic

Gene

accD

Organism
Guizotia abyssinica (Niger) (Ramtilla)
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

[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, 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 bindingi223ZincUniRule annotation1
Metal bindingi226ZincUniRule annotation1
Metal bindingi242ZincUniRule annotation1
Metal bindingi245ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri223 – 245C4-typeUniRule annotationAdd 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

UniPathwayiUPA00655; UER00711

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticUniRule 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
Ordered Locus Names:GuabCp030
Encoded oniPlastid; Chloroplast
OrganismiGuizotia abyssinica (Niger) (Ramtilla)
Taxonomic identifieri4230 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceMillerieaeGuizotia

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003591421 – 483Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplasticAdd BLAST483

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

SMRiB2LMK2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini219 – 483CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST265

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri223 – 245C4-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_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.

B2LMK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRWWFNSML FKKEFEHRCR LSKSTSSLGP IENAIESKDP NINDTDKNIQ
60 70 80 90 100
SWGGHDNYSN VDLFFGVKDI RNFISDDTFL VKDSNGDIYS IYFDIENHIF
110 120 130 140 150
EIDNDHSFCS ELESSFYRNS SYLNNGSKSK NPQHDPYMND TQYTWNNHIN
160 170 180 190 200
SCIDSYLQSQ ICIDSYIVSG SDNSSNNYIS SSICCESGNS SKNADARTSD
210 220 230 240 250
QIIRESSTDL DVTQKYRHLW VQCENCYGLN YKKFFKSKMN LCEQCGYHLK
260 270 280 290 300
MSSSDRIELS IDPGTWEPMD EDMVSLDPIE FHSEEEPYKN RIDSYQRKTG
310 320 330 340 350
LTEAVQTGIG QLDGINVAIA VMDFQFMGGS MGSVVGEKIT RLIEYATKEF
360 370 380 390 400
LPLIIVCASG GARMQEGSLS LMQMAKISSA LYDYQSNKKL FYVPILTSPT
410 420 430 440 450
TGGVTASFGM LGDIIIAEPN AYIAFAGKRV IEQTLNKTVP DGSQAAEYLF
460 470 480
QKGLFDLIVP RNPLKSVLSE LFQLHTFFPL NQN
Length:483
Mass (Da):54,723
Last modified:June 10, 2008 - v1
Checksum:i1B4F970B338A23FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU549769 Genomic DNA Translation: ACB86536.1
RefSeqiYP_001837369.1, NC_010601.1

Genome annotation databases

GeneIDi6219076

Similar proteinsi

Entry informationi

Entry nameiACCD_GUIAB
AccessioniPrimary (citable) accession number: B2LMK2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 10, 2008
Last modified: April 25, 2018
This is version 37 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health