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

Gene

accD

Organism
Cuscuta reflexa (Southern Asian dodder)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

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

Young tissue from this organism is photosynthetic and contains some thylakoids, although the photosynthetic activity does not exceed the light compensation point.Curated

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)
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 bindingi221ZincUniRule annotation1
Metal bindingi224ZincUniRule annotation1
Metal bindingi240ZincUniRule annotation1
Metal bindingi243ZincUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri221 – 243C4-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 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
Synonyms:ycf11, zfpA
Encoded oniPlastid
OrganismiCuscuta reflexa (Southern Asian dodder)
Taxonomic identifieri4129 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeCuscuteaeCuscutaMonogynella

Subcellular locationi

Keywords - Cellular componenti

Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001997831 – 497Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST497

Proteomic databases

PRIDEiP31562

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

ProteinModelPortaliP31562
SMRiP31562
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini217 – 489CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST273

Sequence similaritiesi

Belongs to the AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri221 – 243C4-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.

P31562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERREGGRDN SSCSNVNQLF GVKDSESLLY DDVFIVRDRN GDSYFAYWDI
60 70 80 90 100
EKNTFLSEPF YSYRSRNSSY LPKIKAFMSE DRSQIHEVKN GFRSEDHSKI
110 120 130 140 150
NKINGVENLF HNYNMNVLTD DYNFKMGMNG FHRPQSKIHI NRFIDSYLQS
160 170 180 190 200
QICIATTPGS GSDNDSYIHG SRVYGESESY TRSEGRSSSI RTRTKGVELT
210 220 230 240 250
LRERPGILDR TKKYMYLWLQ CDNCYGLNYK KVLKSKMTIC EQCGYHLQMS
260 270 280 290 300
SSDRIELLID PGTWDPMDED MVSRDPIKFD SGGGEAYKDR LYFYQRKTGL
310 320 330 340 350
TEAVQTGIGQ LNGIPVAIGV MDFKFMGGSM GSVVGEKITR LIEHATNKFL
360 370 380 390 400
PLIIVSASGG ARMQEGSLSL MQMAKISSAL YDYQSNKRLV YVSILTSPTA
410 420 430 440 450
GGVTASFGML GDIIIVEPRA YVAFAGKRVI EQTLNQTIPN DSQEAEFLFH
460 470 480 490
KGLFDLIIPR HLLKSVISEL FTLHDLFPLN QNSNQYSQYR ALLNPIF
Length:497
Mass (Da):56,481
Last modified:October 23, 2007 - v2
Checksum:iE97910C4E8D9E988
GO

RNA editingi

Edited at position 258.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69803 Genomic DNA Translation: CAA49462.1 Sequence problems.
AM711640 Genomic DNA Translation: CAM98405.1 Sequence problems.
PIRiS31477
RefSeqiYP_001430119.1, NC_009766.1

Genome annotation databases

GeneIDi5536593

Keywords - Coding sequence diversityi

RNA editing

Similar proteinsi

Entry informationi

Entry nameiACCD_CUSRE
AccessioniPrimary (citable) accession number: P31562
Secondary accession number(s): A7M977
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 23, 2007
Last modified: May 23, 2018
This is version 98 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

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