ID   A1S5H8_SHEAM            Unreviewed;       940 AA.
AC   A1S5H8;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=Sama_1427 {ECO:0000313|EMBL:ABL99634.1};
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297 {ECO:0000313|EMBL:ABL99634.1, ECO:0000313|Proteomes:UP000009175};
RN   [1] {ECO:0000313|EMBL:ABL99634.1, ECO:0000313|Proteomes:UP000009175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) 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};
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DR   EMBL; CP000507; ABL99634.1; -; Genomic_DNA.
DR   RefSeq; WP_011759542.1; NC_008700.1.
DR   AlphaFoldDB; A1S5H8; -.
DR   STRING; 326297.Sama_1427; -.
DR   KEGG; saz:Sama_1427; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000009175; Chromosome.
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   ECO:0000313|EMBL:ABL99634.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009175};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          598..791
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   940 AA;  104642 MW;  7B481B9B6D1318EE CRC64;
     MHQGSMKAWL ESSHLYGSNA TYVEEMYEAY QEDPTSVSDD WRAVFDNLPP VNGASADVPE
     ASHSKIRDYF RSLAQEGQRK GAGRVTDPEV DAKQVKVLQL INAYRFRGHQ NANLDPLELW
     KRDAVVELDP AFHGLTADDM QREFNTGSFA YGGETLKLGE LVKALKATYC GSIGAEYMHI
     TDTDEKRWIQ QRLEPSMGRA AFDKGVKTRI LEGLNAAEGM EKYLGAKFPG AKRFSLEGGD
     ALVPMMREII YRAGEAGTKE IVVGMAHRGR LNVLVNVLGK RPAELFDEFA GKHAESSGSG
     DVKYHQGFSS DFETPGGNVH LALAFNPSHL EIVNPVVMGS VRARQDRRGC KDGLSVMPIT
     IHGDSAIAGQ GIVQETFNMS QTRGFRVGGS IRIVVNNQVG FTTSNHHDVR STEYCTDIAK
     MVQAPIFHVN ADDPEAVAFV AQVAVDYRNA FKRDVVIDLV CYRRHGHNEA DEPSATQPLM
     YQKIKKHPTP RKIYADRLIA ENAVSADDVT AMINGYRDAL DQGDCVVKEW RPMSLRTVDW
     SPFIGQDWDV SYEPTVALAR LQKLAEKLAY VPETHPLQSR VAKIYADRVA MAKGEKLLDW
     GFAETLAYAT ILEDNNRVRI TGQDSGRGTF FHRHAVLHNQ NDATTYMPLR NLAQEQGPVD
     ITDSVLSEAS VLAFEYGYAT AEPGGLTIWE AQFGDFANCA QVVIDQFLSS GEQKWGRLCG
     LTMLLPHGYE GQGPEHSSAR LERFLQLCAN HNMQVCVPST PAQVYHMLRR QVVRPLRRPL
     VVMSPKSLLR HPLAVSSLEE LANGTFQNVI GEIDSLDPKA VNRVVFCSGK VYFELLERRR
     KENLTNVAII RVEQLYPFPA EEMAAILAEY QHVTDFVWCQ EEPQNQGAWY CSQHHFWAAI
     PKGATLTYAG REAAAAPACG YPELHAHQQE SLVVDALNLK
//