ID G2SYG7_ROSHA Unreviewed; 569 AA.
AC G2SYG7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|HAMAP-Rule:MF_01395};
DE Includes:
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE Short=ACCase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_00823};
DE Includes:
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};
GN Name=accA {ECO:0000256|HAMAP-Rule:MF_00823};
GN Synonyms=accD {ECO:0000256|HAMAP-Rule:MF_01395};
GN OrderedLocusNames=RHOM_14055 {ECO:0000313|EMBL:AEN97917.1};
OS Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN97917.1, ECO:0000313|Proteomes:UP000008178};
RN [1] {ECO:0000313|EMBL:AEN97917.1, ECO:0000313|Proteomes:UP000008178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183
RC {ECO:0000313|Proteomes:UP000008178};
RX PubMed=26543119; DOI=10.1128/genomeA.01286-15;
RA Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL Genome Announc. 3:E0128615-E0128615(2015).
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 -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC First, biotin carboxylase catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC carboxyltransferase to acetyl-CoA to form malonyl-CoA.
CC {ECO:0000256|HAMAP-Rule:MF_00823}.
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|ARBA:ARBA00001072, ECO:0000256|HAMAP-
CC Rule:MF_00823};
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|ARBA:ARBA00004956,
CC ECO:0000256|HAMAP-Rule:MF_00823}.
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_00823}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterotetramer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits of ACCase subunit beta/alpha. {ECO:0000256|ARBA:ARBA00011664}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00823}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000256|HAMAP-
CC Rule:MF_00823}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
CC Rule:MF_01395}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AccA family.
CC {ECO:0000256|ARBA:ARBA00006276}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00010284}.
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DR EMBL; CP003040; AEN97917.1; -; Genomic_DNA.
DR RefSeq; WP_014080884.1; NC_015977.1.
DR AlphaFoldDB; G2SYG7; -.
DR STRING; 585394.RHOM_14055; -.
DR GeneID; 77460356; -.
DR KEGG; rho:RHOM_14055; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_3_0_9; -.
DR OrthoDB; 9772975at2; -.
DR BioCyc; RHOM585394:G1H02-2790-MONOMER; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000008178; 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_00823; AcetylCoA_CT_alpha; 1.
DR HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR NCBIfam; TIGR00513; accA; 1.
DR NCBIfam; NF041504; AccA_sub; 1.
DR NCBIfam; TIGR00515; accD; 1.
DR PANTHER; PTHR42853; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR42853:SF3; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 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_00823}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00823}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00823}; Reference proteome {ECO:0000313|Proteomes:UP000008178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00823}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
FT DOMAIN 26..292
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 299..549
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT ZN_FING 30..52
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395"
SQ SEQUENCE 569 AA; 63105 MW; D94F58CB0FD2B995 CRC64;
MAALFQKRKK EPAEKTPVEA AQALQETIVC PACGREINKK EAEKNLYVCY ECGSYFRVRT
RNRIRMVADA GTFTSWFEDL AEANPLEFPG YEDKVKAAKE KTGLHEAVTI GHCKIYGEDT
VLGICDARFL MSSMGHVMGE KIACAVERAT EEGLPVILFC CSGGARMQEG IVSLMQMAKT
SAALKRHSEA GLLYVPVLTD PTTGGVTASF AMLGDIILAE PGALIGFAGP RVIEQTIGEK
LPEGFQRAQF QLEHGFVDRI VERKELKLTL YRILKLHHKK EGYANFDPVR EADCLEATEL
MKERATKAKA LSAWEKVKAA RKVDRLASVD YIEQIFDEFM ELHGDRQFRD DPAIVGGVAY
LDGQPVTVIG VHKGKDLKEC MHRNYGMPSP EGYRKALRLM KQAEKFKRPV ITFVNTSGAF
CGMEAEERGQ GEAIARNLYE MSGLKVPVLC IMIGEGGSGG ALALSVGNEV WMLENATYSI
LSPEGFASIL WKDGRRAKEA SGVMKITAQD LKALGVIEEI IPEYGMADQP ALISISRYMK
RHIKTFLKKQ NGKTGDQLAA ERYQRFRVF
//
