ID ACCC_ECOLI Reviewed; 449 AA. AC P24182; Q2M8V9; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 2. DT 27-MAR-2024, entry version 210. DE RecName: Full=Biotin carboxylase; DE EC=6.3.4.14 {ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731}; DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305}; GN Name=accC; Synonyms=fabG; OrderedLocusNames=b3256, JW3224; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=K12; RX PubMed=1682920; DOI=10.1073/pnas.88.21.9730; RA Kondo H., Shiratsuchi K., Yoshimoto T., Masuda T., Kitazono A., Tsuru D., RA Anai M., Sekiguchi M., Tanabe T.; RT "Acetyl-CoA carboxylase from Escherichia coli: gene organization and RT nucleotide sequence of the biotin carboxylase subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9730-9733(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1370469; DOI=10.1016/s0021-9258(18)48362-7; RA Li S.-J., Cronan J.E. Jr.; RT "The gene encoding the biotin carboxylase subunit of Escherichia coli RT acetyl-CoA carboxylase."; RL J. Biol. Chem. 267:855-863(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Best E.A., Knauf V.C.; RT "Cloning and characterization of the E. coli fabEG operon encoding subunits RT of acetyl-CoA carboxylase."; RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP PROTEIN SEQUENCE OF 1-12. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160. RX PubMed=2575489; DOI=10.1089/dna.1989.8.779; RA Alix J.-H.; RT "A rapid procedure for cloning genes from lambda libraries by RT complementation of E. coli defective mutants: application to the fabE RT region of the E. coli chromosome."; RL DNA 8:779-789(1989). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=7915138; DOI=10.1021/bi00200a004; RA Waldrop G.L., Rayment I., Holden H.M.; RT "Three-dimensional structure of the biotin carboxylase subunit of acetyl- RT CoA carboxylase."; RL Biochemistry 33:10249-10256(1994). RN [9] {ECO:0007744|PDB:1DV1, ECO:0007744|PDB:1DV2} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP. RX PubMed=10821865; DOI=10.1074/jbc.275.21.16183; RA Thoden J.B., Blanchard C.Z., Holden H.M., Waldrop G.L.; RT "Movement of the biotin carboxylase B-domain as a result of ATP binding."; RL J. Biol. Chem. 275:16183-16190(2000). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ARG-19; GLU-23; RP PHE-363 AND ARG-366. RX PubMed=16793549; DOI=10.1016/j.molcel.2006.04.026; RA Shen Y., Chou C.-Y., Chang G.-G., Tong L.; RT "Is dimerization required for the catalytic activity of bacterial biotin RT carboxylase?"; RL Mol. Cell 22:807-818(2006). RN [11] {ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-444 WILD TYPE AND MUTANT A-296 RP IN COMPLEX WITH ADP; HYDROGENCARBONATE; BIOTIN AND MAGNESIUM, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF RP GLU-296 AND ARG-338. RX PubMed=19213731; DOI=10.1074/jbc.m805783200; RA Chou C.Y., Yu L.P., Tong L.; RT "Crystal structure of biotin carboxylase in complex with substrates and RT implications for its catalytic mechanism."; RL J. Biol. Chem. 284:11690-11697(2009). 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:0000305|PubMed:16793549, ECO:0000305|PubMed:19213731}. 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:0000269|PubMed:16793549, ECO:0000269|PubMed:19213731}; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=115 uM for ATP (at pH 8) {ECO:0000269|PubMed:16793549}; CC KM=16.2 mM for hydrogencarbonate (at pH 8) CC {ECO:0000269|PubMed:19213731}; CC KM=35.1 mM for biotin (at pH 8) {ECO:0000269|PubMed:19213731}; CC Note=kcat is 0.228 sec(-1) with ATP as substrate (at pH 8) CC (PubMed:16793549). kcat is 0.44 sec(-1) with hydrogencarbonate as CC substrate (at pH 8) (PubMed:19213731). kcat is 0.58 sec(-1) with CC biotin as substrate (at pH 8) (PubMed:19213731). CC {ECO:0000269|PubMed:16793549, ECO:0000269|PubMed:19213731}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from CC acetyl-CoA: step 1/1. {ECO:0000305|PubMed:16793549, CC ECO:0000305|PubMed:19213731}. 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:0000269|PubMed:10821865, CC ECO:0000269|PubMed:16793549}. CC -!- INTERACTION: CC P24182; P0ABD8: accB; NbExp=10; IntAct=EBI-542308, EBI-542320; CC P24182; P0A9Q5: accD; NbExp=4; IntAct=EBI-542308, EBI-542064; CC P24182; P16703: cysM; NbExp=3; IntAct=EBI-542308, EBI-542376; CC P24182; P25539: ribD; NbExp=3; IntAct=EBI-542308, EBI-552457; 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; M79446; AAA23748.1; -; Genomic_DNA. DR EMBL; M80458; AAA23409.1; -; Genomic_DNA. DR EMBL; M83198; AAA23746.1; -; Genomic_DNA. DR EMBL; U18997; AAA58059.1; -; Genomic_DNA. DR EMBL; U00096; AAC76288.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77297.1; -; Genomic_DNA. DR EMBL; M32214; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; JS0632; JS0632. DR RefSeq; NP_417722.1; NC_000913.3. DR RefSeq; WP_000884639.1; NZ_STEB01000012.1. DR PDB; 1BNC; X-ray; 2.40 A; A/B=1-449. DR PDB; 1DV1; X-ray; 1.90 A; A/B=1-449. DR PDB; 1DV2; X-ray; 2.50 A; A/B=1-449. DR PDB; 2GPS; X-ray; 2.80 A; A/B=1-449. DR PDB; 2GPW; X-ray; 2.20 A; A/B/C/D=1-449. DR PDB; 2J9G; X-ray; 2.05 A; A/B=1-449. DR PDB; 2V58; X-ray; 2.10 A; A/B=1-449. DR PDB; 2V59; X-ray; 2.40 A; A/B=1-449. DR PDB; 2V5A; X-ray; 2.31 A; A/B=1-449. DR PDB; 2VR1; X-ray; 2.60 A; A/B=1-449. DR PDB; 2W6M; X-ray; 2.00 A; A/B=1-449. DR PDB; 2W6N; X-ray; 1.87 A; A/B=1-449. DR PDB; 2W6O; X-ray; 2.50 A; A/C=1-449. DR PDB; 2W6P; X-ray; 1.85 A; A/B=1-449. DR PDB; 2W6Q; X-ray; 2.05 A; A/B=1-449. DR PDB; 2W6Z; X-ray; 1.90 A; A/B=1-449. DR PDB; 2W70; X-ray; 1.77 A; A/B=1-449. DR PDB; 2W71; X-ray; 1.99 A; A/C=1-449. DR PDB; 3G8C; X-ray; 2.00 A; A/B=1-444. DR PDB; 3G8D; X-ray; 1.90 A; A/B=1-444. DR PDB; 3JZF; X-ray; 2.13 A; A/B=1-449. DR PDB; 3JZI; X-ray; 2.31 A; A/B=1-449. DR PDB; 3RUP; X-ray; 1.99 A; A/B=1-449. DR PDB; 3RV3; X-ray; 1.91 A; A/B=1-449. DR PDB; 3RV4; X-ray; 1.98 A; A=1-449. DR PDB; 4HR7; X-ray; 2.50 A; A/C/E/F=1-449. DR PDB; 6OI9; X-ray; 2.06 A; A/B=1-449. DR PDBsum; 1BNC; -. DR PDBsum; 1DV1; -. DR PDBsum; 1DV2; -. DR PDBsum; 2GPS; -. DR PDBsum; 2GPW; -. DR PDBsum; 2J9G; -. DR PDBsum; 2V58; -. DR PDBsum; 2V59; -. DR PDBsum; 2V5A; -. DR PDBsum; 2VR1; -. DR PDBsum; 2W6M; -. DR PDBsum; 2W6N; -. DR PDBsum; 2W6O; -. DR PDBsum; 2W6P; -. DR PDBsum; 2W6Q; -. DR PDBsum; 2W6Z; -. DR PDBsum; 2W70; -. DR PDBsum; 2W71; -. DR PDBsum; 3G8C; -. DR PDBsum; 3G8D; -. DR PDBsum; 3JZF; -. DR PDBsum; 3JZI; -. DR PDBsum; 3RUP; -. DR PDBsum; 3RV3; -. DR PDBsum; 3RV4; -. DR PDBsum; 4HR7; -. DR PDBsum; 6OI9; -. DR AlphaFoldDB; P24182; -. DR SMR; P24182; -. DR BioGRID; 4262456; 269. DR BioGRID; 852073; 6. DR ComplexPortal; CPX-3206; Acetyl-CoA carboxylase complex. DR DIP; DIP-9035N; -. DR IntAct; P24182; 20. DR STRING; 511145.b3256; -. DR BindingDB; P24182; -. DR DrugBank; DB08314; (2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE. DR DrugBank; DB08315; 2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE. DR DrugBank; DB08074; 3-(3-Methyl-2-buten-1-yl)-3H-purin-6-amine. DR DrugBank; DB08075; 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine. DR DrugBank; DB08076; 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine. DR DrugBank; DB08316; 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one. DR DrugBank; DB08317; 5-methyl-6-phenylquinazoline-2,4-diamine. DR DrugBank; DB08144; 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine. DR DrugBank; DB08145; 6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE. DR DrugBank; DB08318; 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine. DR DrugBank; DB08146; 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine. DR jPOST; P24182; -. DR PaxDb; 511145-b3256; -. DR EnsemblBacteria; AAC76288; AAC76288; b3256. DR GeneID; 75206104; -. DR GeneID; 947761; -. DR KEGG; ecj:JW3224; -. DR KEGG; eco:b3256; -. DR PATRIC; fig|511145.12.peg.3355; -. DR EchoBASE; EB0272; -. DR eggNOG; COG0439; Bacteria. DR HOGENOM; CLU_000395_3_2_6; -. DR InParanoid; P24182; -. DR OMA; FINKPKH; -. DR OrthoDB; 9763189at2; -. DR PhylomeDB; P24182; -. DR BioCyc; EcoCyc:BIOTIN-CARBOXYL-MONOMER; -. DR BioCyc; MetaCyc:BIOTIN-CARBOXYL-MONOMER; -. DR BRENDA; 6.3.4.14; 2026. DR SABIO-RK; P24182; -. DR UniPathway; UPA00655; UER00711. DR EvolutionaryTrace; P24182; -. DR PRO; PR:P24182; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IDA:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; IC:EcoliWiki. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. 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; IDA:EcoliWiki. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc. DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:ComplexPortal. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IDA:ComplexPortal. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:EcoliWiki. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2. 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; Direct protein sequencing; KW Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis; KW Lipid metabolism; Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..449 FT /note="Biotin carboxylase" FT /id="PRO_0000146791" 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:0000269|PubMed:19213731" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:10821865, FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, FT ECO:0007744|PDB:3G8D" FT BINDING 159 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D" FT BINDING 165..166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:10821865, FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, FT ECO:0007744|PDB:3G8D" FT BINDING 201..204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:10821865, FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, FT ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D" FT BINDING 209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C" FT BINDING 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:10821865, FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, FT ECO:0007744|PDB:3G8C" FT BINDING 238 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C" FT BINDING 276 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C" FT BINDING 276 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C" 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:10821865, FT ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, FT ECO:0007744|PDB:3G8D" FT BINDING 288 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D" 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:0000255|PROSITE-ProRule:PRU00409" 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:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C" FT BINDING 295 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C" FT BINDING 338 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C" FT BINDING 338 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /evidence="ECO:0000269|PubMed:19213731, FT ECO:0007744|PDB:3G8C" FT MUTAGEN 19 FT /note="R->E: Loss of homodimerization. No effect on ATP FT binding." FT /evidence="ECO:0000269|PubMed:16793549" FT MUTAGEN 23 FT /note="E->R: Loss of homodimerization. No effect on ATP FT binding." FT /evidence="ECO:0000269|PubMed:16793549" FT MUTAGEN 296 FT /note="E->A: Severe reduction in catalytic activity." FT /evidence="ECO:0000269|PubMed:19213731" FT MUTAGEN 338 FT /note="R->A: Severe reduction in catalytic activity." FT /evidence="ECO:0000269|PubMed:19213731" FT MUTAGEN 363 FT /note="F->A: Loss of homodimerization. No effect on ATP FT binding." FT /evidence="ECO:0000269|PubMed:16793549" FT MUTAGEN 366 FT /note="R->E: Loss of homodimerization. No effect on ATP FT binding." FT /evidence="ECO:0000269|PubMed:16793549" FT CONFLICT 136 FT /note="G -> A (in Ref. 7)" FT /evidence="ECO:0000305" FT CONFLICT 160 FT /note="A -> P (in Ref. 7)" FT /evidence="ECO:0000305" FT CONFLICT 260..261 FT /note="CA -> SR (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="L -> M (in Ref. 1; AAA23748)" FT /evidence="ECO:0000305" FT STRAND 3..7 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 11..24 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 27..33 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 40..44 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:2W70" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 63..73 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:2W70" FT TURN 84..87 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 89..97 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 107..114 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 116..126 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 142..152 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:2W70" FT TURN 165..168 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 175..193 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 198..202 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 208..216 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:2W6O" FT STRAND 222..234 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 237..244 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 250..267 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 271..280 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 283..290 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 297..304 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 308..317 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 332..340 FT /evidence="ECO:0007829|PDB:2W70" FT TURN 344..346 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 365..368 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 383..394 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 395..408 FT /evidence="ECO:0007829|PDB:2W70" FT STRAND 410..414 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 418..425 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 428..432 FT /evidence="ECO:0007829|PDB:2W70" FT HELIX 439..444 FT /evidence="ECO:0007829|PDB:2W70" SQ SEQUENCE 449 AA; 49321 MW; 68C55F10ACB4F170 CRC64; MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL QIRIMNDENF QHGGTNIHYL EKKLGLQEK //