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ACCD_RHOBA
ID   ACCD_RHOBA              Reviewed;         312 AA.
AC   Q7UHX0;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=RB12904;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC       Note=Binds 1 zinc ion per subunit. {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; BX294155; CAD77847.1; -; Genomic_DNA.
DR   RefSeq; NP_870770.1; NC_005027.1.
DR   RefSeq; WP_007327662.1; NC_005027.1.
DR   AlphaFoldDB; Q7UHX0; -.
DR   SMR; Q7UHX0; -.
DR   STRING; 243090.RB12904; -.
DR   EnsemblBacteria; CAD77847; CAD77847; RB12904.
DR   KEGG; rba:RB12904; -.
DR   PATRIC; fig|243090.15.peg.6254; -.
DR   eggNOG; COG0777; Bacteria.
DR   HOGENOM; CLU_015486_1_1_0; -.
DR   InParanoid; Q7UHX0; -.
DR   OMA; PEGLWIK; -.
DR   OrthoDB; 504557at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001025; 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:0008270; F:zinc ion binding; 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   InterPro; IPR041010; Znf-ACC.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF17848; zf-ACC; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00515; accD; 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; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..312
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta"
FT                   /id="PRO_0000389832"
FT   DOMAIN          55..312
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   ZN_FING         59..81
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ   SEQUENCE   312 AA;  33739 MW;  A640FBCF54E89135 CRC64;
     MEMDTAVENP AVEKNGQPTP SSTSTATDAA PTPNAPNRPA PNTAGNRKRG VPEGVWRKCD
     SCGASLFYKE VQQRLNVCPQ CDHHFYVSAW ERVAQVLDDG TFEPMNEHLR PTDPLEFRDR
     RSYAERLVGE QKRTGLTDAV LTGTGMIRAR RVAFAVTDSA FIMGSMGSVV GERLTRLIER
     ATEQNLALII ISASGGGARM HEGILSLMQM AKVSAALSRY HAAGGLFISV LTNPTMGGVA
     ASFASLGDLV FAEPKALIGF AGPRTIKATI GIELPEGFQT SEFLLEHGYI DRIVHRKSLK
     TEIATAIDYC GK
 
 
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