GenomeNet

Database: UniProt
Entry: D3DJ41
LinkDB: D3DJ41
Original site: D3DJ41 
ID   2OCL_HYDTT              Reviewed;         652 AA.
AC   D3DJ41; Q05KD8;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   16-JAN-2019, entry version 52.
DE   RecName: Full=2-oxoglutarate carboxylase large subunit {ECO:0000312|EMBL:BAI69843.1};
DE            EC=6.4.1.7;
DE   AltName: Full=2-oxoglutarate carboxylase alpha subunit {ECO:0000303|PubMed:14731279};
GN   Name=cfiA {ECO:0000312|EMBL:BAI69843.1};
GN   OrderedLocusNames=HTH_1392, Hydth_1382;
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:BAF34932.1}
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] {ECO:0000312|EMBL:BAI69843.1}
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.,
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] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-30, SUBUNIT, AND BIOTINYLATION.
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:
CC       Reaction=2-oxoglutarate + ATP + hydrogencarbonate = ADP + H(+) +
CC         oxalosuccinate + phosphate; Xref=Rhea:RHEA:20425,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58931,
CC         ChEBI:CHEBI:456216; EC=6.4.1.7;
CC         Evidence={ECO:0000269|PubMed:17076668};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q58628};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q58628};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:Q58628};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large subunits and 8 small
CC       subunits. {ECO:0000269|PubMed:14731279,
CC       ECO:0000269|PubMed:17076668}.
CC   -!- PTM: Biotinylated. {ECO:0000269|PubMed:14731279}.
DR   EMBL; AB246889; BAF34932.1; -; Genomic_DNA.
DR   EMBL; AP011112; BAI69843.1; -; Genomic_DNA.
DR   EMBL; CP002221; ADO45767.1; -; Genomic_DNA.
DR   RefSeq; WP_012964023.1; NC_017161.1.
DR   ProteinModelPortal; D3DJ41; -.
DR   SMR; D3DJ41; -.
DR   STRING; 608538.HTH_1392; -.
DR   EnsemblBacteria; ADO45767; ADO45767; Hydth_1382.
DR   EnsemblBacteria; BAI69843; BAI69843; HTH_1392.
DR   KEGG; hte:Hydth_1382; -.
DR   KEGG; hth:HTH_1392; -.
DR   PATRIC; fig|608538.5.peg.1413; -.
DR   eggNOG; ENOG4107QSA; Bacteria.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG5016; LUCA.
DR   HOGENOM; HOG000231389; -.
DR   KO; K20140; -.
DR   OMA; ELHLHCH; -.
DR   OrthoDB; 361205at2; -.
DR   BioCyc; HTHE608538:G1GOC-1412-MONOMER; -.
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:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Biotin; Complete proteome; Direct protein sequencing;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    652       2-oxoglutarate carboxylase large subunit.
FT                                /FTId=PRO_0000402797.
FT   DOMAIN       26    288       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN      563    643       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION       34     38       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P11498}.
FT   METAL        35     35       Divalent metal cation.
FT                                {ECO:0000250|UniProtKB:P11498}.
FT   METAL       196    196       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250|UniProtKB:P11498}.
FT   METAL       227    227       Divalent metal cation.
FT                                {ECO:0000250|UniProtKB:P11498}.
FT   METAL       229    229       Divalent metal cation.
FT                                {ECO:0000250|UniProtKB:P11498}.
FT   BINDING     105    105       Substrate.
FT                                {ECO:0000250|UniProtKB:P11498}.
FT   BINDING     362    362       Substrate.
FT                                {ECO:0000250|UniProtKB:P11498}.
FT   MOD_RES     196    196       N6-carboxylysine.
FT                                {ECO:0000250|UniProtKB:P11498}.
FT   MOD_RES     609    609       N6-biotinyllysine.
FT                                {ECO:0000250|UniProtKB:P11498,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   652 AA;  72546 MW;  8D6C35B018DF9921 CRC64;
     MQAVEIMEEI REKFKEFEKG GFRKKILITD LTPRDGQQCK LATRVRTDDL LPLCEAMDKV
     GFYAVEVWGG ATYDVCLRYL KEDPWERLRR IKEVMPNTKL QMLFRGQNIV GYRPKSDKLV
     YKFVERAIKN GITVFRVFDA LNDNRNIKTA VKAIKELGGE AHAEISYTRS PIHTYQKWIE
     YALEIAEMGA DWLSFKDATG IIMPFETYAI IKGIKEATGG KLPVLLHNHD MSGTAIVNHM
     MAVLAGVDML DTVLSPLAFG SSHPATESVV AMLEGTPFDT GIDMKKLDEL AEIVKQIRKK
     YKKYETEYAG VNAKVLIHKI PGGMISNMVA QLIEANALDK IEEALEEVPN VERDLGHPPL
     LTPSSQIVGV QAVLNVISGE RYKVITKEVR DYVEGKYGKP PGPISKELAE KILGPGKEPD
     FSIRAADLAD PNDWDKAYEE TKAILGREPT DEEVLLYALF PMQAKDFFVA REKGELHPEP
     VDELVETTEV KAGVVPGAAP VEFEIVYHGE KFKVKVEGVS AHQEPGKPRK YYIRVDGRLE
     EVQITPHVEA IPKGGPTPTA VQAEEKGIPK ATQPGDATAP MPGRVVRVLV KEGDKVKEGQ
     TVAIVEAMKM ENEIHAPISG VVEKVFVKPG DNVTPDDALL RIKHIEEEVS YG
//
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