ID ACCC2_POPTR Reviewed; 526 AA. AC B9N843; U5FKU1; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 19-FEB-2014, sequence version 2. DT 24-JAN-2024, entry version 85. DE RecName: Full=Biotin carboxylase 2, chloroplastic; DE EC=6.3.4.14 {ECO:0000250|UniProtKB:O04983}; DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A 2 {ECO:0000305}; DE Flags: Precursor; GN ORFNames=POPTR_0018s14250g; OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. OS trichocarpa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus. OX NCBI_TaxID=3694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nisqually; RX PubMed=16973872; DOI=10.1126/science.1128691; RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W., RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M., RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S., RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A., RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S., RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y., RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S., RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F., RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O., RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J., RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y., RA Rokhsar D.S.; RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."; RL Science 313:1596-1604(2006). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Nisqually; RG US DOE Joint Genome Institute (JGI-PGF); RA Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S., RA Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., Pitluck S., RA Chapman J., Putnam N.H., Brunner A., Busov V., Campbell M., Chalot M., RA Covert S., Davis J., DiFazio S., Gribskov M., Gunter L., Hamberger B., RA Jansson S., Joshi C., Larimer F., Martin F., Napoli C., Nelson D., RA Ralph S., Rombauts S., Rouze P., Schrader J., Tsai C., Vahala J., RA Tuskan G., Rokhsar D.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A CC carboxylase complex; first, biotin carboxylase catalyzes the CC carboxylation of the carrier protein and then the transcarboxylase CC transfers the carboxyl group to form malonyl-CoA. CC {ECO:0000250|UniProtKB:O04983}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, CC ChEBI:CHEBI:456216; EC=6.3.4.14; CC Evidence={ECO:0000250|UniProtKB:O04983}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00969}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00969}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000255|PROSITE-ProRule:PRU00969}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from CC acetyl-CoA: step 1/1. 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:0000305}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. 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; CM009307; ERP49997.1; -; Genomic_DNA. DR RefSeq; XP_006372200.1; XM_006372138.1. DR AlphaFoldDB; B9N843; -. DR SMR; B9N843; -. DR STRING; 3694.B9N843; -. DR GeneID; 18107844; -. DR KEGG; pop:18107844; -. DR eggNOG; KOG0238; Eukaryota. DR HOGENOM; CLU_000395_3_2_1; -. DR InParanoid; B9N843; -. DR OrthoDB; 1129179at2759; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000006729; Chromosome 18. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR005481; BC-like_N. DR InterPro; IPR011764; Biotin_carboxylation_dom. DR InterPro; IPR005482; Biotin_COase_C. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR011054; Rudment_hybrid_motif. DR NCBIfam; TIGR00514; accC; 1. DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1. DR Pfam; PF02785; Biotin_carb_C; 1. DR Pfam; PF00289; Biotin_carb_N; 1. DR Pfam; PF02786; CPSase_L_D2; 1. DR SMART; SM00878; Biotin_carb_C; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS50979; BC; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. PE 2: Evidence at transcript level; KW ATP-binding; Biotin; Chloroplast; Fatty acid biosynthesis; KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; Plastid; KW Reference proteome; Transit peptide. FT TRANSIT 1..71 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 72..526 FT /note="Biotin carboxylase 2, chloroplastic" FT /id="PRO_0000391774" FT DOMAIN 185..382 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT ACT_SITE 357 FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 213..274 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 223 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 229..230 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 265..268 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 273 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 302 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 340 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 340 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 340 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 353 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 353 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 353 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 353 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 353 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 355 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 355 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969" FT BINDING 357 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 360 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 403 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 403 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" SQ SEQUENCE 526 AA; 57497 MW; CAC6A56109E42892 CRC64; MEATLPVCKS VTSTPGLFMK RNSGIRNSQC SFMVGTKVNF PRQRTQATQA NHCAKKNGGA LGVTCRAEKI LVANRGEIAV RVIRTAHELG IPCVAVYSTI DKDALHVKLA DESVCIGEAP SNQSYLVIQN VLSAAISRGC TMLHPGYGFL AENAVFVEMC REHGINFIGP NPDSIRVMGD KSTARETMKK ANVPTVPGSD GLLQSTEEAV KLASEIGYPV MIKATAGGGG RGMRLAKEPD EFVKLLQQAK SEAAAAFGND GVYLEKYVQN PRHIEFQVLA DKFGNVVHFG ERDCSIQRRN QKLLEEAPSP ALTPELRKAM GDAAVAAAAS IGYIGVGTVE FLLDERGSFY FMEMNTRIQV EHPVTEMISS VDLIEEQIRV AMGEKIQYKQ EDIVLRGHSI ECRINAEDAF KGFRPGPGRI TAYLPSGGPF VRMDSHVYPD YVVPPSYDSL LGKLIVWAPT REKAIERMKR ALDDTIITGV PTTIDYHKLI LDIEDFKNGN VDTAFIPKHE QELAAPQQII LANSAS //