ID A3QDH4_SHELP Unreviewed; 940 AA.
AC A3QDH4;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN OrderedLocusNames=Shew_1655 {ECO:0000313|EMBL:ABO23522.1};
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO23522.1, ECO:0000313|Proteomes:UP000001558};
RN [1] {ECO:0000313|EMBL:ABO23522.1, ECO:0000313|Proteomes:UP000001558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) 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; CP000606; ABO23522.1; -; Genomic_DNA.
DR RefSeq; WP_011865454.1; NC_009092.1.
DR AlphaFoldDB; A3QDH4; -.
DR STRING; 323850.Shew_1655; -.
DR KEGG; slo:Shew_1655; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000001558; 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:ABO23522.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001558};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 599..792
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 940 AA; 105204 MW; 7A0096C9E1A39A0E CRC64;
MHQGIMKAWL ESSHLNGANS TYVEEMYEAY QEDPQSVSED WRAVFDNLPY ANGATADVPE
AAHSKVREYF RSLALDGRHK SAARVTDPEV DAKQVKVLQL INAYRFRGHQ NANLDPLGLW
KRDTVSELDP AFHGLTGEDM EREFNTGSFA HGGDTMKLGD LVKALKATYC AAIGAEYMHI
TDTDEKRWIQ QRLEPSLGRA NYDKNTKTRI LEGLNAAEGM EKYLGAKFPG AKRFSLEGGD
ALVPMMREII YRGGEAGTKE IVVGMAHRGR LNLLVNILGK KPSELFDEFA GKHSDELNGS
GDVKYHQGFS SDFETPGGNV HLALAFNPSH LEIVNPVVMG SVRARLDRRG CKTGLQVMPI
TVHGDSAIAG QGIVQETFNM SQTRAFKVGG SIRIVVNNQV GFTTNLTEDT RSTEYCTDIA
KMVQAPIFHV NADDPESVAF VAQLAVDYRN EFKRDVVIDL VCYRRHGHNE ADEPSATQPL
MYAKIKKHPT PRKIYADRLI EEQTLGADDV TAMINDYRDA LDKGDCVVKE WRPMTLHTVD
WTPYLNREWD EAYPAELPLD RVKALADKIS YVPESHKLQS RVAKIYKDRV AMAAGDKLLD
WGFAETLAYA SILDDNKRVR ITGQDSGRGT FFHRHAVLHN QNDATAYLPL RHLSDMQGPI
DISDSVLSEA SVLAFEYGYA TAEPGGLTIW EAQFGDFANC AQVVIDQFLS SGEQKWGRLC
GLTMLLPHGY EGQGPEHSSA RLERFLQLCA NHNMQVCVPS TPAQVYHMLR RQVVRPMRRP
LVVMSPKSLL RHPLAVSSLE ELAEGTFQNV IAEIDELDSS KVDRVVFCSG KVYFELLEKR
RKENLDNVAL IRVEQLYPFP HEDMAQILAQ YQHVKDFVWC QEEPQNQGAW YCSQHHFWAA
IPAGAQLTYA GREASAAPAC GYPALHTQQQ ESLINSALKL
//
