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 27-MAR-2024, entry version 69.
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; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC 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-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., 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, 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 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: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 subunits.
CC {ECO:0000269|PubMed:14731279, ECO:0000269|PubMed:17076668}.
CC -!- PTM: Biotinylated. {ECO:0000269|PubMed:14731279}.
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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 AlphaFoldDB; D3DJ41; -.
DR SMR; D3DJ41; -.
DR STRING; 608538.HTH_1392; -.
DR KEGG; hte:Hydth_1382; -.
DR KEGG; hth:HTH_1392; -.
DR PATRIC; fig|608538.5.peg.1413; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_2_0; -.
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:UniProtKB-KW.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 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; Direct protein sequencing; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..652
FT /note="2-oxoglutarate carboxylase large subunit"
FT /id="PRO_0000402797"
FT DOMAIN 26..288
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 563..643
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT BINDING 34..38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT BINDING 196
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT BINDING 227
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT BINDING 229
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT MOD_RES 196
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P11498"
FT MOD_RES 609
FT /note="N6-biotinyllysine"
FT /evidence="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
//
