ID A0A8A9WFV0_9LAMI Unreviewed; 491 AA. AC A0A8A9WFV0; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 28-JUN-2023, entry version 8. DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {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:QTT58215.1}; OS Ruellia brittoniana. OG Plastid; Chloroplast {ECO:0000313|EMBL:QTT58215.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Acanthaceae; Acanthoideae; Ruellieae; OC Ruelliinae; Ruellia; New World Ruellia. OX NCBI_TaxID=440931 {ECO:0000313|EMBL:QTT58215.1}; RN [1] {ECO:0000313|EMBL:QTT58215.1} RP NUCLEOTIDE SEQUENCE. RA Tang H.H., Feng S.S., Liu Z.Z.; RL Submitted (MAR-2021) 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, biotin carboxylase and two subunits each of CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD). CC {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000256|HAMAP- CC Rule:MF_01395}. CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP- CC Rule:MF_01395}. 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; MW697905; QTT58215.1; -; Genomic_DNA. DR AlphaFoldDB; A0A8A9WFV0; -. DR UniPathway; UPA00655; UER00711. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell. 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. DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. 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 TIGRFAMs; TIGR00515; accD; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01395}; Chloroplast {ECO:0000313|EMBL:QTT58215.1}; 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 Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01395}; Plastid {ECO:0000313|EMBL:QTT58215.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01395}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01395}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}. FT DOMAIN 281..445 FT /note="Acetyl-CoA carboxylase" FT /evidence="ECO:0000259|Pfam:PF01039" FT ZN_FING 228..250 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT REGION 26..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..52 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 228 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 250 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" SQ SEQUENCE 491 AA; 55617 MW; 6C5F7EDABC53A5C7 CRC64; MERWWFNSMP FKKELEHRYG IKKSTANAGP IENTSESEDS NRKGRAKSIH SLRNHDNSSY SGVDLLFGVK DIRNFISDDT FLVRDSNGDN YSIYIENQIF EIDNNHSFLS ELQSSFSGYH NSSYRNNVST SEDSLYNRYM YDTQSSWNNH ITSCIDSYLQ SQFSIDTSIV SDSSDGYISR CVFDKRTTNN ESKRSSIRTE EKSSDLTLRE RSNDLDATQN YRHLWVQCEN CYGLNYKRFL KSKMNICEQC GYHLKISSSE RIEVSIDPGT WDPMDEDMVS LDPIGFHSEE EPYKDRIDSY QRKTGLTEAV QTGIGQLNGV PVALGVMDFQ FMGGSMGSVV GEKITRLIEY ATDRFIPLII VCASGGARMQ EGSLSLMQMA KISSALYDYQ SNKKLFYVSI LTSPTTGGVT ASFGMLGDII IAEPNSYIAF AGKRVIEQTL NKTVPEGSQV AEYLFQKGLF DLIVPRNLLK SVLSELFKLH AFFPVNSNSI K //