2OCS_HYDTT
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 03-AUG-2022, entry version 75.
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; Aquificae; Aquificales; Aquificaceae; 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}.
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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 EnsemblBacteria; BAI69844; BAI69844; 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; IGPKHYS; -.
DR OrthoDB; 361205at2; -.
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 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 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; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 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 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
