ID 2OCS_HYDTT Reviewed; 472 AA. AC D3DJ42; Q05KD9; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 1. DT 24-JAN-2024, entry version 81. DE RecName: Full=2-oxoglutarate carboxylase small subunit {ECO:0000312|EMBL:BAI69844.1}; DE EC=6.4.1.7; DE AltName: Full=2-oxoglutarate carboxylase beta subunit {ECO:0000303|PubMed:14731279}; GN Name=cfiB {ECO:0000312|EMBL:BAI69844.1}; GN OrderedLocusNames=HTH_1393, Hydth_1383; OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; OC Hydrogenobacter. OX NCBI_TaxID=608538; RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF34931.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=17076668; DOI=10.1111/j.1365-2958.2006.05399.x; RA Aoshima M., Igarashi Y.; RT "A novel oxalosuccinate-forming enzyme involved in the reductive RT carboxylation of 2-oxoglutarate in Hydrogenobacter thermophilus TK-6."; RL Mol. Microbiol. 62:748-759(2006). RN [2] {ECO:0000312|EMBL:BAI69844.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6534 / IAM 12695 / TK-6; RX PubMed=20348262; DOI=10.1128/jb.00158-10; RA Arai H., Kanbe H., Ishii M., Igarashi Y.; RT "Complete genome sequence of the thermophilic, obligately RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter RT thermophilus TK-6."; RL J. Bacteriol. 192:2651-2652(2010). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6534 / IAM 12695 / TK-6; RX PubMed=21677850; DOI=10.4056/sigs.1463589; RG US DOE Joint Genome Institute (JGI-PGF); RA Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J., Tice H., RA Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Ngatchou-Djao O.D., Land M., Hauser L., Jeffries C.D., RA Han C., Detter J.C., Ubler S., Rohde M., Tindall B.J., Goker M., Wirth R., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., RA Kyrpides N.C.; RT "Complete genome sequence of Hydrogenobacter thermophilus type strain (TK- RT 6)."; RL Stand. Genomic Sci. 4:131-143(2011). RN [4] {ECO:0000305} RP PROTEIN SEQUENCE OF 1-30, AND SUBUNIT. RX PubMed=14731279; DOI=10.1046/j.1365-2958.2003.03863.x; RA Aoshima M., Ishii M., Igarashi Y.; RT "A novel biotin protein required for reductive carboxylation of 2- RT oxoglutarate by isocitrate dehydrogenase in Hydrogenobacter thermophilus RT TK-6."; RL Mol. Microbiol. 51:791-798(2004). CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + ATP + hydrogencarbonate = (S)-oxalosuccinate CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:20425, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:153066, ChEBI:CHEBI:456216; CC EC=6.4.1.7; Evidence={ECO:0000269|PubMed:17076668}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:O27939}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:O27939}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000250|UniProtKB:O27939}; CC -!- SUBUNIT: Heterohexadecamer of 8 large subunits and 8 small subunits. CC {ECO:0000269|PubMed:14731279, ECO:0000269|PubMed:17076668}. 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; AB246889; BAF34931.1; -; Genomic_DNA. DR EMBL; AP011112; BAI69844.1; -; Genomic_DNA. DR EMBL; CP002221; ADO45768.1; -; Genomic_DNA. DR RefSeq; WP_012964024.1; NC_017161.1. DR PDB; 7KBL; X-ray; 2.30 A; A/B=1-472. DR PDB; 7KC7; X-ray; 2.20 A; A/B=1-472. DR PDB; 7KCT; X-ray; 2.02 A; A/B=1-472. DR PDBsum; 7KBL; -. DR PDBsum; 7KC7; -. DR PDBsum; 7KCT; -. DR AlphaFoldDB; D3DJ42; -. DR SMR; D3DJ42; -. DR STRING; 608538.HTH_1393; -. DR KEGG; hte:Hydth_1383; -. DR KEGG; hth:HTH_1393; -. DR PATRIC; fig|608538.5.peg.1414; -. DR eggNOG; COG0439; Bacteria. DR HOGENOM; CLU_000395_3_2_0; -. DR OMA; MYYDSMI; -. DR OrthoDB; 9807469at2; -. DR Proteomes; UP000002574; Chromosome. DR GO; GO:0034029; F:2-oxoglutarate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. 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; 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:SF1; BIOTIN CARBOXYLASE; 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; Ligase; KW Magnesium; Nucleotide-binding; Reference proteome. FT CHAIN 1..472 FT /note="2-oxoglutarate carboxylase small subunit" FT /id="PRO_0000402798" FT DOMAIN 1..445 FT /note="Biotin carboxylation" FT /evidence="ECO:0000255" FT DOMAIN 119..316 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT ACT_SITE 291 FT /evidence="ECO:0000250|UniProtKB:P24182, ECO:0000255" FT BINDING 115 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT BINDING 199 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P24182" FT STRAND 3..7 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 11..23 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 27..32 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 40..44 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 62..72 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:7KCT" FT TURN 83..86 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 88..96 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 106..111 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 115..124 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 140..150 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 159..163 FT /evidence="ECO:0007829|PDB:7KBL" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 173..191 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 206..214 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 220..227 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 235..242 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 248..264 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 269..277 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 296..303 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 307..315 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 331..341 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 365..369 FT /evidence="ECO:0007829|PDB:7KCT" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:7KBL" FT STRAND 384..394 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 395..408 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 418..426 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 428..431 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 439..442 FT /evidence="ECO:0007829|PDB:7KCT" FT HELIX 444..447 FT /evidence="ECO:0007829|PDB:7KCT" SQ SEQUENCE 472 AA; 53386 MW; 18648BB7E22E6C02 CRC64; MFKKVLVANR GEIACRVIRA CKELGIQTVA IYNEIESTAR HVKMADEAYM IGVNPLDTYL NAERIVDLAL EVGAEAIHPG YGFLAENEHF ARLCEEKGIT FIGPHWKVIE LMGDKARSKE VMKRAGVPTV PGSDGILKDV EEAKRIAKEI GYPVLLKASA GGGGRGIRIC RNEEELVRNY ENAYNEAVKA FGRGDLLLEK YIENPKHIEF QVLGDKYGNV IHLGERDCSI QRRNQKLVEI APSLLLTPEQ REYYGSLVVK AAKEIGYYSA GTMEFIADEK GNLYFIEMNT RIQVEHPVTE MITGVDIVKW QIRIAAGERL RYSQEDIRFN GYSIECRINA EDPKKGFAPS IGTIERYYVP GGFGIRVEHA SSKGYEITPY YDSLIAKLIV WAPLWEVAVD RMRSALETYE ISGVKTTIPL LINIMKDKDF RDGKFTTRYL EEHPHVFDYA EHRDKEDFVA FISAVIASYH GL //