ID ACCC_HAEIN Reviewed; 448 AA. AC P43873; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 150. DE RecName: Full=Biotin carboxylase; DE EC=6.3.4.14 {ECO:0000250|UniProtKB:P24182}; DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305}; GN Name=accC; OrderedLocusNames=HI_0972; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] {ECO:0007744|PDB:4MV1, ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4, ECO:0007744|PDB:4MV6, ECO:0007744|PDB:4MV7, ECO:0007744|PDB:4MV8, ECO:0007744|PDB:4MV9, ECO:0007744|PDB:4RZQ} RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) IN COMPLEX WITH ADP; ATP ANALOGS AND RP MAGNESIUM. RX PubMed=26020841; DOI=10.1021/acs.biochem.5b00340; RA Broussard T.C., Pakhomova S., Neau D.B., Bonnot R., Waldrop G.L.; RT "Structural Analysis of Substrate, Reaction Intermediate, and Product RT Binding in Haemophilus influenzae Biotin Carboxylase."; RL Biochemistry 54:3860-3870(2015). 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:P24182}. 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:P24182}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00409}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00409}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000255|PROSITE-ProRule:PRU00409}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from CC acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:P24182}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl CC carrier protein, biotin carboxylase and the two subunits of carboxyl CC transferase in a 2:2 complex. {ECO:0000250|UniProtKB:P24182}. 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; L42023; AAC22632.1; -; Genomic_DNA. DR PIR; F64105; F64105. DR RefSeq; NP_439133.1; NC_000907.1. DR PDB; 4MV1; X-ray; 1.91 A; A=1-448. DR PDB; 4MV3; X-ray; 1.69 A; A=1-448. DR PDB; 4MV4; X-ray; 1.61 A; A=1-448. DR PDB; 4MV6; X-ray; 1.77 A; A=1-448. DR PDB; 4MV7; X-ray; 1.73 A; A=1-448. DR PDB; 4MV8; X-ray; 2.06 A; A=1-448. DR PDB; 4MV9; X-ray; 1.98 A; A=1-448. DR PDB; 4RZQ; X-ray; 1.98 A; A=1-448. DR PDB; 6OI8; X-ray; 2.50 A; A=1-448. DR PDB; 6OJH; X-ray; 2.05 A; A=1-448. DR PDBsum; 4MV1; -. DR PDBsum; 4MV3; -. DR PDBsum; 4MV4; -. DR PDBsum; 4MV6; -. DR PDBsum; 4MV7; -. DR PDBsum; 4MV8; -. DR PDBsum; 4MV9; -. DR PDBsum; 4RZQ; -. DR PDBsum; 6OI8; -. DR PDBsum; 6OJH; -. DR AlphaFoldDB; P43873; -. DR SMR; P43873; -. DR STRING; 71421.HI_0972; -. DR EnsemblBacteria; AAC22632; AAC22632; HI_0972. DR KEGG; hin:HI_0972; -. DR PATRIC; fig|71421.8.peg.1013; -. DR eggNOG; COG0439; Bacteria. DR HOGENOM; CLU_000395_3_2_6; -. DR OrthoDB; 9763189at2; -. DR PhylomeDB; P43873; -. DR BioCyc; HINF71421:G1GJ1-1013-MONOMER; -. DR BRENDA; 6.3.4.14; 2529. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000579; Chromosome. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Biotin; Fatty acid biosynthesis; KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..448 FT /note="Biotin carboxylase" FT /id="PRO_0000146793" FT DOMAIN 1..445 FT /note="Biotin carboxylation" FT DOMAIN 120..317 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT ACT_SITE 292 FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:26020841, FT ECO:0007744|PDB:4MV8" FT BINDING 159 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:26020841, FT ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4" FT BINDING 165..166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 201..204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:26020841, FT ECO:0007744|PDB:4MV1, ECO:0007744|PDB:4MV3, FT ECO:0007744|PDB:4MV4, ECO:0007744|PDB:4MV8, FT ECO:0007744|PDB:4RZQ" FT BINDING 209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 238 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 276 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:26020841, FT ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4" FT BINDING 276 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:26020841, FT ECO:0007744|PDB:4MV4" FT BINDING 276 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 288 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:26020841, FT ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:26020841, FT ECO:0007744|PDB:4MV4" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 288 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 288 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 290 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:26020841, FT ECO:0007744|PDB:4MV4" FT BINDING 290 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 292 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 295 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 338 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 338 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000250|UniProtKB:P24182" FT STRAND 4..7 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 11..24 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 27..33 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 40..44 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 45..55 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:4MV4" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 63..73 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:4MV4" FT TURN 84..87 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 89..97 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 107..114 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 116..126 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 142..152 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 169..172 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 175..192 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 198..202 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 208..216 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 222..234 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 237..244 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 250..267 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 271..280 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 283..290 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 297..304 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 308..316 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 332..342 FT /evidence="ECO:0007829|PDB:4MV4" FT TURN 344..346 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 365..368 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 384..394 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 395..408 FT /evidence="ECO:0007829|PDB:4MV4" FT STRAND 410..414 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 418..425 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 428..432 FT /evidence="ECO:0007829|PDB:4MV4" FT HELIX 439..444 FT /evidence="ECO:0007829|PDB:4MV4" SQ SEQUENCE 448 AA; 49108 MW; 2B497E2A31ED96D1 CRC64; MLEKVVIANR GEIALRILRA CKELGIKTVA VHSTADRDLK HVLLADETIC IGPAPSAKSY LNIPAIIAAA EVTGADAIHP GYGFLSENAD FAEQVERSGF TFIGPTADVI RLMGDKVSAI KAMKKAGVPC VPGSDGPVSN DIAKNKEIAK RIGYPIIIKA SGGGGGRGMR VVRSEDALEE SIAMTKAEAK AAFNNDMVYM EKYLENPRHV EIQVLADTHG NAVYLAERDC SMQRRHQKVV EEAPAPGITE EVRRDIGSRC ANACVEIGYR GAGTFEFLYE NGEFYFIEMN TRIQVEHPVT EMITGVDLVK EQLRIAAGLP ISFKQEDIKV KGHAMECRIN AEDPKTFLPS PGKVNHLHSP GGLGVRWDSH VYGGYTVPPH YDSMIAKLIT YGDTREVAIR RMQNALSETI IDGIKTNIPL HELILEDENF QKGGTNIHYL EKKLGMNE //