ID A0A285QY94_9SPHN Unreviewed; 728 AA.
AC A0A285QY94;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN ORFNames=SAMN06297144_1630 {ECO:0000313|EMBL:SOB86524.1};
OS Sphingomonas guangdongensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1141890 {ECO:0000313|EMBL:SOB86524.1, ECO:0000313|Proteomes:UP000219494};
RN [1] {ECO:0000313|EMBL:SOB86524.1, ECO:0000313|Proteomes:UP000219494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12672 {ECO:0000313|EMBL:SOB86524.1,
RC ECO:0000313|Proteomes:UP000219494};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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 -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR EMBL; OBMI01000002; SOB86524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285QY94; -.
DR Proteomes; UP000219494; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000219494}.
FT DOMAIN 393..574
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 728 AA; 77571 MW; D20D7B506E99E15B CRC64;
MIDAAEAVHQ KLVRRLRERD LPAIGVERGG LTLTDLAELF HSQVASRQLD RLSRRLQARG
EGFYTIGSSG HEGNAAVARA ARVTDMAFLH YRSAAFQIER SKQLPGETPT WDMLLSFAAS
SEDPIAGGRH KVIGSKRLAI PPQTSTIASH LPKAVGAAFA LGLARRMGVA PSVPADSVII
ASFGDASANH STAQGAFNTA GWAAHQGTPL PIVFLCEDNG IGISTATPHG WIEAQFRARA
GLHYVACDGT DVVDAYRGAR AAIDHARRTK RPVFLHMSTV RLYGHAGSDV QATYRQRAAI
EAEEERDPLL RTAAYLLADG VPADELLAIY DRAEATLARA AELAIARPKL DSAAAVMASI
VPPPASPPPA RAPSTEERTA LFARDAGQID KPQHMARLLS WALADLMLQH PEIVVAGEDV
GPKGGVYNVT ARLHERFGSA RVVNTLLDEQ SILGLAIGCG HVGLLPIPEI QFLAYVHNAE
DQIRGEAATL PFFSQGQFTN PMVVRIAGLP YQKGFGGHFH NDNSLAVFRD VPGVVLAVPS
SGADAVAMLR ECVRLAQEEG RVVIFIEPIA LYMTRDLHAE GDGLMTAIYA SDSTPVRLGE
VGVHDDGEAL AIVTYGNGAF LSRQAQPLLA AAGIDARVID LRWLAPLPAE ALLAAVGTRP
RVLIVDECRS TGSQSEALMA FFTEKAPDKR VARIAAEDSF IPLGKGATLT LPSRDGIVAA
ARALIARG
//
