ID V8G6S4_9BURK Unreviewed; 953 AA.
AC V8G6S4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=V757_05405 {ECO:0000313|EMBL:ETD72239.1};
OS Pelistega indica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pelistega.
OX NCBI_TaxID=1414851 {ECO:0000313|EMBL:ETD72239.1, ECO:0000313|Proteomes:UP000018766};
RN [1] {ECO:0000313|EMBL:ETD72239.1, ECO:0000313|Proteomes:UP000018766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM-7 {ECO:0000313|EMBL:ETD72239.1,
RC ECO:0000313|Proteomes:UP000018766};
RA Kumbhare S.V., Shetty S.A., Sharma O., Dhotre D.P.;
RT "Genomic analysis of Pelistega sp. HM-7.";
RL Submitted (NOV-2013) 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:ETD72239.1}.
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DR EMBL; AYSV01000071; ETD72239.1; -; Genomic_DNA.
DR RefSeq; WP_023950527.1; NZ_CABMIG010000071.1.
DR AlphaFoldDB; V8G6S4; -.
DR PATRIC; fig|1414851.3.peg.1093; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000018766; 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:UP000018766};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 599..796
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 953 AA; 106180 MW; F0783D6BECBDA6AB CRC64;
MTTAIEKSNN SYLFGSNVSY VEEQYEAYLE NPESVTPEWR DYFDKLSHLP AVDGSETTRD
QNHSSIIASF AQRAKANTLL VQAAPASLEV AGKQLKVQSL IAAYRSLGVR HAILDPLKRS
ERPEIPELDP AFYGLTDADL DEVYSATNTY FTTNSTMTLR EILNSLRDTY CRSVGSEFMH
ISDPKAKRWI QERLESTLST AALTVAEKKN LLKQVTEAEG LERFLHTKYV GQKRFSLEGG
ESFIACMDEV VNHGGKIGVQ EMVVGMAHRG RLNMLINIMG KRPGDLFAEF EGKHAEGLTD
GDVKYHNGFS SDISTAGGPV HLSLAFNPSH LEIVNPVVEG SARARQDRRQ NKKQVLPVLV
HGDAAFAGQG VVMETLNLAQ TRGYGTGGTL HVVINNQIGF TTSDPRDARS TLYCTDVVKM
IEAPVFHVNG DDPEAVAFVT RLAMDYRAEF AHDVVIDIVC YRKLGHNEQD TPALTQPLMY
KSISKHPGTR QLYADKLVAQ GVLQANEPDD LVKEYRAVMD AGGETAEPVL TDVKNQFAID
WKPFIGAKWT DKADTAVPTA ELKRLGERIT TIPETFTPHK LVEKLLADRR AMANGEMNLD
WGMGEHLAFA SLVNAGFNIR ITGQDAGRGT FTHRHAVLHD QKRERWDDGT YIPLQSISEN
QAKFLVIDSV LSEEAVLGFE YGFACSEPNT LTIWEAQFGD FANGAQVVID QFIASGEAKW
GRQCGLALML PHGYEGQGPE HSSARIERFL QLCADNNMQV VQPTNGAQIF HLLRRQMIRN
FRKPLVIFTP KSLLRNKDAS VPLTELSEGS FKTVIGEVDT AINADKVTRL LVCSGKVYYD
LVNARKEREA SDVAIIRIEQ LYPFAHKDFE AEFEKYPHVK EVVWVQDEPQ NQGPWFYVQH
HIYENMKKGQ KLAYAGRAAS SSPAVGYLAK HIEQQKALIE QAFAARIKPV LSK
//
