ID A0A1T4QIU6_9BACT Unreviewed; 913 AA.
AC A0A1T4QIU6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=SAMN04488132_108158 {ECO:0000313|EMBL:SKA03614.1};
OS Sediminibacterium ginsengisoli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Sediminibacterium.
OX NCBI_TaxID=413434 {ECO:0000313|EMBL:SKA03614.1, ECO:0000313|Proteomes:UP000190888};
RN [1] {ECO:0000313|EMBL:SKA03614.1, ECO:0000313|Proteomes:UP000190888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22335 {ECO:0000313|EMBL:SKA03614.1,
RC ECO:0000313|Proteomes:UP000190888};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FUWH01000008; SKA03614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4QIU6; -.
DR STRING; 413434.SAMN04488132_108158; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000190888; 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 Reference proteome {ECO:0000313|Proteomes:UP000190888};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 578..771
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 913 AA; 103163 MW; B304093B8498DC3F CRC64;
MKDFSYITNS HPAYIENLYQ EFVKDPSAVD QDLRKFFEGF DFAVTSNGTA ATGSQSSAPA
AGTDWMSEIR VYRLILGYRN KGHLLAKTNP IRQRKDRGAN LELSFFGLSE ADMDKTFQAG
NLLGLGATSL RNILAHLQQS YSGSVGIEFK YISDQKKVDW LVAEMEKGFK VPIAIEKKKR
ILEKLNQGVM FEKFLHTKYI GQKRFSLEGG ETTIAALDAV ITTAANNDVQ EVVIGMAHRG
RLNVLANVMG KTYEQIFSEF EGTAAIDQTM GSGDVKYHMG YGSEVQTADN KTIHLKLMPN
PSHLEAVDPV VVGFARAKAD VLYKSDFDRI LPILIHGDAS VAGQGVVYEV LQMCNLQGYY
TGGTIHFVIN NQIGFTTDFD DARSADYCTS AAAMVQAPVL HVNGDDAEAV VKCAEIATRY
RQEFNSDIFI DMVCYRRHGH NEGDDPKYTQ PQLYALIDKH QNPREIYTQF LKENGEPDAQ
ELAKEMEKKF WADLQERLDE VKQHPLPYNY QQPELVWKSL RKAGESDFDQ SPVTAISESQ
VKSMFDRLMQ WPADFKPLKK VEKLLQDKIK LLDSEQKIDW ATAELLAYGS ILTEGNIVRM
SGQDVKRGTF SHRHAVLRDE DNNKEYNRLD HFQEQQEKFR IYNSLLSEYG VLGFEYGYAM
ANPNALVIWE AQFGDFCNGA QTMIDQFLAA GEQKWQRQNG VVMLLPHGYE GQGPEHSSAR
MERFLQLCAE LNMVVTNITT ASNLFHAFRR QLAWPFRKPL INFSPKANLR NPNTYSHISE
FSGGGFKEVI DDAFATDAAE VKKVLLCSGK LYYELADRQQ KENRKDIAIV RMEQLYPIPQ
KQLDALYKKY SKATWFWVQE EPLNMGAAAF LKMNLNSINF GVISRNASAA TATGYSKVHA
QEQAEIIETA FAI
//
