ID A0A2G0CJN7_9BACT Unreviewed; 925 AA.
AC A0A2G0CJN7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=CGL56_03845 {ECO:0000313|EMBL:PHL00182.1};
OS Neolewinella marina.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Neolewinella.
OX NCBI_TaxID=438751 {ECO:0000313|EMBL:PHL00182.1, ECO:0000313|Proteomes:UP000226437};
RN [1] {ECO:0000313|EMBL:PHL00182.1, ECO:0000313|Proteomes:UP000226437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKG-38 {ECO:0000313|EMBL:PHL00182.1,
RC ECO:0000313|Proteomes:UP000226437};
RA Wang K.;
RT "The draft genome sequence of Lewinella marina KCTC 32374.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PHL00182.1}.
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DR EMBL; PDLO01000001; PHL00182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G0CJN7; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000226437; 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:UP000226437};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 582..775
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 925 AA; 104679 MW; 16352BB4971221CB CRC64;
MSNYSHLANA HPGYIEQLYR QYSESPDSVD ASWRDFFLGF DYASEKSPTG PGMPTTPEGT
IDWEHVKKEL SVFALIKAYR MRGHVASNID PIQEFEDPDA GLELSDFDLG EEDLDKPFRA
ADQFFMPEGS TLRQIVDNLK RIYLGSIGFE TDHIFHREKR RWLRERIEKH HPEEAYGLQL
DDKRHILETL NDAVGFEDFL KTKYPAQKRF GLEGGEAAIV ALNTIISEAA RDGVEEVVIG
MAHRGRLNVL ANIMGKSYES IFQEFEGVIP DNIKGDGDVK YHMGYSSLIE TRVGKPVNVK
LAPNPSHLEA VAPVVEGFAR AKADVLYGND YDKIVPILVH GDAAVAGQGV VFETAQMSGL
EAYTTGGSIH LIINNQIGFT TDYEDARTSI YASGVATVIE APVFHVNGDD PEAVYYVAKL
AMEYRNEFNS DVFIDMLCYR KNGHNEGDDP GYTQPGMYER VKRHPDVRQV YTDRLVARKD
VQAKLAKEMA KKFKSRLQSV HTKVKNSDLP YSYQPPEKAW SMLNRDHWSY EHFSESPETG
VPLEQMKNIL RHITTLPEGF EPVNKVNRLY NNYEQSVSSD QLDWALGELS AYATLLMDGH
SVRMSGQDVR RGTFSHRHAV LKSQDGESIY NRLDGLSDDQ GKMHIYNSLL SEYAVLGFEY
GYSTASPENL VIWEAQFGDF ANGAMTVFDQ FISSGESKWG RMSGLTVFLP HGYEGQGPEH
SSARLERFLQ LCAEYNMVVA NVTMPANLFH LLRRQLTWNF RKPLILMSPK SGLRHEMAVS
SIDDFGPGTR FQEVIDDPTV KDPAKVTRVL LCSGKVYFDL AKHKAAEEAE GVAIVRMEQL
FPLPIRQLQE VRERYPNAKD YRWVQEESRN AGAWSYISEQ FLYNTDLGFE QKLDYVGRPA
SASPATGYKP VHVKQQKRLV DQAFE
//