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Entry: I3C5F9_9FLAO
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Original site: I3C5F9_9FLAO 
ID   I3C5F9_9FLAO            Unreviewed;       334 AA.
AC   I3C5F9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=JoomaDRAFT_1853 {ECO:0000313|EMBL:EIJ38852.1};
OS   Joostella marina DSM 19592.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Joostella.
OX   NCBI_TaxID=926559 {ECO:0000313|EMBL:EIJ38852.1, ECO:0000313|Proteomes:UP000004690};
RN   [1] {ECO:0000313|EMBL:EIJ38852.1, ECO:0000313|Proteomes:UP000004690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19592 {ECO:0000313|EMBL:EIJ38852.1,
RC   ECO:0000313|Proteomes:UP000004690};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Ovchinnikova G., Kyrpides N., Mavromatis K.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Improved High-Quality Draft genome of Joostella marina DSM 19592.";
RL   Submitted (FEB-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. {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   -!- 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01395}.
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DR   EMBL; JH651379; EIJ38852.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3C5F9; -.
DR   STRING; 926559.JoomaDRAFT_1853; -.
DR   eggNOG; COG0777; Bacteria.
DR   HOGENOM; CLU_015486_1_0_10; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000004690; 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: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|HAMAP-Rule:MF_01395};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004690};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01395}.
FT   DOMAIN          73..334
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
SQ   SEQUENCE   334 AA;  37608 MW;  5F57748C55875075 CRC64;
     MPPANFFFLW RLSYISRHLR DTDRKNYLTH SDVKYREIKL DKGLNYTKNM AWFKRKEKGI
     QTTTQEKKDT PKGLWYKSPT GKIVEADELA KNFYVSPEDD YHVRIGSKEY FSILFDDNKF
     KELDPNLESK DPLSFVDTKK YSDRLKQAQE KTALKDAVRT AVGKSKGKEL VIACMDFAFI
     GGSMGSVVGE KIARAIDDAI KKKVPFVMIS KSGGARMMEA ALSLMQLAKT SAKLAQLSDL
     GIPYISLCTD PTTGGTTASY AMLGDINIAE PGALIGFAGP RVVKEATGKD LPENFQTSEF
     LLEHGFLDFI THRRDLKSKI NQYIDLILNQ PMRA
//
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