ACCD_HIRBI
ID ACCD_HIRBI Reviewed; 346 AA.
AC C6XMV9;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN Name=accD {ECO:0000255|HAMAP-Rule:MF_01395}; OrderedLocusNames=Hbal_2343;
OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hirschia.
OX NCBI_TaxID=582402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418;
RX PubMed=21705585; DOI=10.1128/jb.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC transcarboxylase to acetyl-CoA to form malonyl-CoA. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC (AccD). {ECO:0000255|HAMAP-Rule:MF_01395}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01395}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; CP001678; ACT60023.1; -; Genomic_DNA.
DR RefSeq; WP_015828173.1; NC_012982.1.
DR AlphaFoldDB; C6XMV9; -.
DR SMR; C6XMV9; -.
DR STRING; 582402.Hbal_2343; -.
DR EnsemblBacteria; ACT60023; ACT60023; Hbal_2343.
DR KEGG; hba:Hbal_2343; -.
DR eggNOG; COG0777; Bacteria.
DR HOGENOM; CLU_015486_1_0_5; -.
DR OrthoDB; 504557at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000002745; Chromosome.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..346
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit beta"
FT /id="PRO_0000389756"
FT DOMAIN 24..292
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT REGION 300..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 37320 MW; 6F7C6B6F06E3FFAC CRC64;
MSWLTNLPPG LKNVFGKKDT PENLWIKCPK SGDLVYKDDL EASLFVTPAG AHLRVGPDLR
FKSMFDGSEY EELELPEVVK DPLKFKDDRK YVDRLKSSRA KTGREDCMAA AIGKIGKQNA
VVLVQDFAFM GGSLGMAAGE AFITAAEKAL ETKSALIICT ASGGARMQEG ALSLMQMPRT
TVAITELKDA SLPYIVVLTD PTTGGVAASY AMIGDIHIGE PEAMVAFAGA RVIEQTIREK
LPEGFQRAEF LRERGMVDMV VDRRDLPAKL GQILSMLMGG KPLPEVEPIA VADVEELEAA
EAEAAPDEVV EVEAPAVDEI VEEKPAATKA KPRSKAKSKA APKTDE
