ID   G9ZJG3_9GAMM            Unreviewed;       933 AA.
AC   G9ZJG3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=HMPREF9080_02932 {ECO:0000313|EMBL:EHM49882.1};
OS   Cardiobacterium valvarum F0432.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Cardiobacterium.
OX   NCBI_TaxID=797473 {ECO:0000313|EMBL:EHM49882.1, ECO:0000313|Proteomes:UP000004750};
RN   [1] {ECO:0000313|EMBL:EHM49882.1, ECO:0000313|Proteomes:UP000004750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0432 {ECO:0000313|EMBL:EHM49882.1,
RC   ECO:0000313|Proteomes:UP000004750};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHM49882.1}.
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DR   EMBL; AGCM01000191; EHM49882.1; -; Genomic_DNA.
DR   RefSeq; WP_006986916.1; NZ_JH417970.1.
DR   AlphaFoldDB; G9ZJG3; -.
DR   STRING; 797473.HMPREF9080_02932; -.
DR   PATRIC; fig|797473.3.peg.2378; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   Proteomes; UP000004750; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          597..790
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   933 AA;  104112 MW;  F74C1B41AB0B1B74 CRC64;
     MGNYQTQRAT SQLSGGNAAY IETLYEQYLD APDSVAAGWR AYFDSIRAGA SNEKPRLPVQ
     ERFEAMADLP DLPGGEADPE AIAKQVAVLG LISGYRTRGH QAADLCPIHL RPRREVPDID
     YRWHGLTDAD LDRTFNTGTL FSGDMTLRDI IAYLDKTYKH HIGAEILHIH TTEERRWLQE
     RLEKAANGYG YSDEEKRAFL QQLVAADGLE KYLHKRFVGQ KRFSLEGGDG LIPLTETLIN
     RLGASGSKEI GIAMAHRGRL NMLINILGKR PADLFDEFEG KYTPQGGRSG DVKYHMGFSS
     SVETAGGLVD LTLAYNPSHL EFVNPVMQGS MRARIERAQE ERQADHLFAD NYAVPIQIHG
     DAAFAGQGVN LETLQLSQVR GYRVGGTLHI IVNNQIGFTT SNPLDTRSAM YCSDAAKLIQ
     APVLHVNGDD PEALAFAGEI AVDYLRTFHK DIFIDIVCYR RLGHNEADEP SATQPMMYKK
     IRAHDVPAKV YADRLIAEGV IAAGDYQKLQ DDYRARLEAG EAVTRSLPRR ADDPLRLAWK
     ALSNQDWNAP VNTAYPREAL TRLGEKIYTL PDDFVPHPIV EKLMAARLDM VRGKAPLDWG
     AAENLAYASL LEQRYSVRVS GEDCGRGTFS HRHAVIHDQT TGDSYTPLAH LYDGQPNVRI
     IDSILSECAV LGFEYGYSTA EPQGLTIWEA QFGDFANGAQ VIIDQFITSG EAKWGRYSGL
     TMLLPHGYEG QGPEHSSARI ERYLQLCADN NVQVCVPTTP AQIFHLLRRQ VLRRFRKPLI
     AISPKSLLRH KLAVSDLSEL AEGHFRPVLG EKDTLKAADN IRRVILCSGK VYYDLLQKRR
     DENIDDIAIL RLEQLYPFPE AELAVMLAPY TNADIIWCQE EPRNQGAWRQ IYEWLAPALP
     ANKKPQYIGR AASASTAAGY LKMHNAEQAA LDA
//