GenomeNet

Database: UniProt
Entry: A0A0P8W518_9CLOT
LinkDB: A0A0P8W518_9CLOT
Original site: A0A0P8W518_9CLOT 
ID   A0A0P8W518_9CLOT        Unreviewed;       305 AA.
AC   A0A0P8W518;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
DE            EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000256|HAMAP-Rule:MF_01395,
GN   ECO:0000313|EMBL:KPU42669.1};
GN   ORFNames=OXPF_38460 {ECO:0000313|EMBL:KPU42669.1};
OS   Oxobacter pfennigii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX   NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU42669.1, ECO:0000313|Proteomes:UP000050326};
RN   [1] {ECO:0000313|EMBL:KPU42669.1, ECO:0000313|Proteomes:UP000050326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU42669.1,
RC   ECO:0000313|Proteomes:UP000050326};
RA   Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT   "Genome sequence of Oxobacter pfennigii DSM 3222.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01395};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01395};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01395};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01395}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPU42669.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LKET01000062; KPU42669.1; -; Genomic_DNA.
DR   RefSeq; WP_054876806.1; NZ_LKET01000062.1.
DR   AlphaFoldDB; A0A0P8W518; -.
DR   STRING; 36849.OXPF_38460; -.
DR   PATRIC; fig|36849.3.peg.4064; -.
DR   OrthoDB; 9772975at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000050326; Unassembled WGS sequence.
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_beta.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   NCBIfam; TIGR00515; accD; 1.
DR   PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_01395};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_01395}; Ligase {ECO:0000313|EMBL:KPU42669.1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_01395};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01395}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050326};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01395}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
FT   DOMAIN          53..305
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   ZN_FING         57..79
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ   SEQUENCE   305 AA;  33386 MW;  00F27CD4C711B6D6 CRC64;
     MLKDLFRKRQ YATISLTKDE VYGVTANSNN KSAEANKAIP HSEKKTQIIV DENSIQCKNC
     ESIVSKETMK NSASVCPVCG HHGRIGAKVR LELIADCDSF EELYKNIETL NPLEYAEYEE
     KIKKSREQSG LNEAVLTGKC TIDGMKALIG IMDSNFIMGS MGSVVGEKLT RLIEKAMDDK
     LPVIVFCASG GARMQEGILS LMQMAKVSAA LKKLSDGGLL FIPVLTDPTT GGVTASFAML
     GDIIIAEPGA LIGFAGKRVI EQTIRQKLPE GFQTSEFLQE HGFIDLIVSR HDLKDTLSKL
     LKLHN
//
DBGET integrated database retrieval system