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 06-MAR-2013, entry version 28. DE RecName: Full=2-oxoglutarate carboxylase small subunit; DE EC=6.4.1.7; DE AltName: Full=2-oxoglutarate carboxylase beta subunit; GN Name=cfiB; OrderedLocusNames=HTH_1393, Hydth_1383; OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6). OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter. OX NCBI_TaxID=608538; RN [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- RT 6."; RL Mol. Microbiol. 62:748-759(2006). RN [2] 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., RA Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., RA Chen A., Palaniappan K., Ngatchou-Djao O.D., Land M., Hauser L., RA Jeffries C.D., Han C., Detter J.C., Ubler S., Rohde M., Tindall B.J., RA Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Hydrogenobacter thermophilus type strain RT (TK-6)."; RL Stand. Genomic Sci. 4:131-143(2011). RN [4] 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 RT thermophilus TK-6."; RL Mol. Microbiol. 51:791-798(2004). CC -!- CATALYTIC ACTIVITY: ATP + 2-oxoglutarate + HCO(3)(-) = ADP + CC phosphate + oxalosuccinate. CC -!- COFACTOR: Magnesium or manganese or cobalt (By similarity). CC -!- SUBUNIT: Heterohexadecamer of 8 large subunits and 8 small CC subunits. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. CC -!- SIMILARITY: Contains 1 biotin carboxylation domain. 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; YP_003433045.1; NC_013799.1. DR RefSeq; YP_005512061.1; NC_017161.1. DR ProteinModelPortal; D3DJ42; -. DR SMR; D3DJ42; 1-451. DR GeneID; 12100253; -. DR GeneID; 8773244; -. DR GenomeReviews; AP011112_GR; HTH_1393. DR KEGG; hte:Hydth_1383; -. DR KEGG; hth:HTH_1393; -. DR PATRIC; 32211731; VBIHydThe36152_1404. DR HOGENOM; HOG000008988; -. DR KO; K01959; -. DR OMA; MADEAYM; -. DR ProtClustDB; CLSK2299734; -. DR GO; GO:0034029; F:2-oxoglutarate carboxylase activity; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR011764; Biotin_carboxylation_dom. DR InterPro; IPR005482; Biotin_COase_C. DR InterPro; IPR005481; CarbamoylP_synth_lsu_N. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02785; Biotin_carb_C; 1. DR Pfam; PF00289; CPSase_L_chain; 1. DR Pfam; PF02786; CPSase_L_D2; 1. DR SMART; SM00878; Biotin_carb_C; 1. DR SUPFAM; SSF52440; PreATP-grasp-like; 1. DR SUPFAM; SSF51246; Rudmnt_hyb_motif; 1. DR TIGRFAMs; TIGR00514; accC; 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 ATP-binding; Biotin; Complete proteome; Direct protein sequencing; KW Ligase; Magnesium; Nucleotide-binding. FT CHAIN 1 472 2-oxoglutarate carboxylase small subunit. FT /FTId=PRO_0000402798. FT DOMAIN 1 445 Biotin carboxylation. FT DOMAIN 119 316 ATP-grasp. FT ACT_SITE 291 291 Potential. FT BINDING 115 115 ATP (By similarity). FT BINDING 199 199 ATP (By similarity). 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 //