ID K9UKG1_CHAP6 Unreviewed; 290 AA.
AC K9UKG1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ORFNames=Cha6605_3716 {ECO:0000313|EMBL:AFY94689.1};
OS Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC Chamaesiphon.
OX NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY94689.1, ECO:0000313|Proteomes:UP000010366};
RN [1] {ECO:0000313|EMBL:AFY94689.1, ECO:0000313|Proteomes:UP000010366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Chamaesiphon sp. PCC 6605.";
RL Submitted (MAY-2012) 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.
CC {ECO:0000256|ARBA:ARBA00025280, ECO:0000256|HAMAP-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|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01395}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
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DR EMBL; CP003600; AFY94689.1; -; Genomic_DNA.
DR AlphaFoldDB; K9UKG1; -.
DR STRING; 1173020.Cha6605_3716; -.
DR KEGG; cmp:Cha6605_3716; -.
DR PATRIC; fig|1173020.3.peg.4260; -.
DR eggNOG; COG0777; Bacteria.
DR HOGENOM; CLU_015486_1_1_3; -.
DR OrthoDB; 9772975at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000010366; 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_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 InterPro; IPR041010; Znf-ACC.
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 Pfam; PF17848; zf-ACC; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01395}; 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};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01395}; Reference proteome {ECO:0000313|Proteomes:UP000010366};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01395};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01395};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_01395}.
FT DOMAIN 33..290
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT ZN_FING 37..59
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ SEQUENCE 290 AA; 32276 MW; 2A3CBF6B56123E57 CRC64;
MPQLGSLFDW FADRQKTSPS IQQQQEREIA DGLWTKCESC NAIAYTKDLI ANQMVCLECG
HHKRVSCHER ISQLIDDDTW IPLDEQLQPT DPLKFKDRKA YSDRLRETQR KTGLTDAVVT
GMGKIEGSPI ALGVMDFRFM GGSMGSVVGE KLTRAIEHAT ANRIAVAIVC ASGGARMQEG
MLSLMQMAKI SGALERHREA QLLYLPILTH PTTGGVIASF AMLGDIILAE PKATIGFAGR
RVIEQTLREK LPDDFQTSEY LLKKGFVDKI VPRTQLKHTV AQLVRLHTRA
//
