ID A0A7W5D188_9ACTN Unreviewed; 748 AA. AC A0A7W5D188; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. 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=accD {ECO:0000256|HAMAP-Rule:MF_01395}; GN Synonyms=accA {ECO:0000256|HAMAP-Rule:MF_00823}; GN ORFNames=FHR31_000865 {ECO:0000313|EMBL:MBB3171053.1}; OS Parvibacter caecicola. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Parvibacter. OX NCBI_TaxID=747645 {ECO:0000313|EMBL:MBB3171053.1, ECO:0000313|Proteomes:UP000530850}; RN [1] {ECO:0000313|EMBL:MBB3171053.1, ECO:0000313|Proteomes:UP000530850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22242 {ECO:0000313|EMBL:MBB3171053.1, RC ECO:0000313|Proteomes:UP000530850}; RA Klenk H.-P.; RT "Sequencing the genomes of 1000 actinobacteria strains."; RL Submitted (AUG-2020) 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 -!- 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}. 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:MBB3171053.1}. 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; JACHYA010000002; MBB3171053.1; -; Genomic_DNA. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000530850; Unassembled WGS sequence. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC. 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; IPR005481; BC-like_N. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR011763; COA_CT_C. DR InterPro; IPR011762; COA_CT_N. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR PANTHER; PTHR42853; PTHR42853; 1. DR Pfam; PF03255; ACCA; 1. DR Pfam; PF00289; Biotin_carb_N; 1. DR PRINTS; PR01069; ACCCTRFRASEA. DR SUPFAM; SSF52096; SSF52096; 2. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00513; accA; 1. 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}; Ligase {ECO:0000313|EMBL:MBB3171053.1}; 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}; 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 188..454 FT /note="CoA carboxyltransferase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50980" FT DOMAIN 462..728 FT /note="CoA carboxyltransferase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50989" FT ZN_FING 192..214 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT REGION 459..489 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..483 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 192 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT METAL 195 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT METAL 211 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT METAL 214 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" SQ SEQUENCE 748 AA; 80990 MW; AD0CF1B685765C6A CRC64; MPKQYVDIVP EQQAVAASVA EEVRAPEAPQ PGDGSLLVSM VGVIAEQLAK AQHGRPRVLV MAQGKMARRS LAAIRETGVW TVVPQAGDWR LDINPKLADE AARLGQKPLR QLFYNAYAVL QAAQEAQVCA VFLDGPCAFL ASDNRFLSRA AEAGIGVFAA FEDDVTRQYW TERVPAAADV PGAPQPTWWR TCHSCKLTFD DAQFVANDYH CPHCGTLDRM GSRERIDLIL DDGVFEEWDA DLPDADPLSF PGYGEKVAAQ RAKTGLHEAV VCGFGHIGRV PCAFGCMDSG FFMGSMGSFV GEKLARLFDR ATEQGLPVVV FCASGGARMQ EGLASLMQMA KVSCAIERHS RAGLLFISVL TDPTTGGVTA SFATLGDVIL AEPKTLIGFA GQRVIRDTIK QELPEGFQTA EFALQHGLID AIVERTEMRR AIKTLLRLHC GTPPHPEEEA DEVLKAGAQA PLSEKDRRKL ERHAQRELRR AGLKGAPEPG SAWERVQLAR NVHRPTALTY ISGITESFFE LHGDRAFADD EAIVAGVGMV GGQPVTIIAQ EKGSNLNDRI RRNFGCPMPE GYRKSARLMQ QAQKFGRPIV CLVDTQGAFC GTEAEERGQG NAIAENLKLM AGLTVPVVSV LLGEGGSGGA LALAVSNRVA MQENAVYSIL SPEGFASILW KDGKRAPEAA EVMQMDAARV FELGFVDEVL SEGEGPAHEN PEEAVENVLA YLEEALVEMA PLSPEELVTQ RQARFAQF //