ID   A0A136NMW7_9BACT        Unreviewed;       912 AA.
AC   A0A136NMW7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=UZ10_BCD003000426 {ECO:0000313|EMBL:KXK47515.1};
OS   Bacteroidetes bacterium OLB10.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617421 {ECO:0000313|EMBL:KXK47515.1, ECO:0000313|Proteomes:UP000070480};
RN   [1] {ECO:0000313|EMBL:KXK47515.1, ECO:0000313|Proteomes:UP000070480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB10 {ECO:0000313|EMBL:KXK47515.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK47515.1}.
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DR   EMBL; LNBX01000013; KXK47515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136NMW7; -.
DR   STRING; 1617421.UZ10_BCD003000426; -.
DR   PATRIC; fig|1617421.3.peg.445; -.
DR   Proteomes; UP000070480; 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   ECO:0000313|EMBL:KXK47515.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          574..767
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          881..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..901
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   912 AA;  103404 MW;  4FD0EE779667821C CRC64;
     MEKKRTYLGN ADPTAIEELY NKYLQNSQSV DETWRDFFDG FDFARVNTAG ATDTVSNVAS
     AHLEKEFKVL RLINDYRDRG HLFTATNPVR DRRKYFPTLD IENFGLTKED MSTVFQAGNE
     IGIGPATLAA IISHLHDTYC ASIGVEYKYI RHPEVVKWLE QKMESTRNRM EFSIADKKRI
     LQKLNEAVVF ENFLQLKFTG QKRFSLEGAE TTIPALDAIL EYGADMGIKE FTIGMSHRGR
     LNVLANILNK SYEDIFTEFE GKEFDDNAFD GDVKYHLGFS SDLTTANGKK LHVAVIPNPS
     HLEAVDAVVQ GIVRAKIDAQ GGTVNDIAPI LIHGDAAIAG QGIVYEVIQM SLLKGYSTGG
     TIHLIINNQV GFTTNYIDAR SSTYCTDVAK VTLSPVFHVN GDNAEALIYT IKLALEYRQK
     YHRDVFVDIL CYRKYGHNEG DEPRFTQPLL YKAIATHPNP REIYTQKLLS QGEIEAGLAK
     EMEKEFKALL QSKLDASTKI EKAKIDSFKE GAWNKLRFSQ PEDFLKQPAT SVDKDTLLSI
     ADKMTNLPAD KKFFSKITRL FNERKEMMKG DGRLDWAMGE LLAYGTLLNE GNSVRLSGQD
     CERGTFSHRH AVVRVEDSEE QYTPLNHISD KQAPFYIFNS HLSEYGVLGF DYGYGFASPN
     SLVLWEAQFG DFSNGAQIII DQYLSSAEDK WKRMNGIVML LPHGYEGQGA EHSSARMERY
     LTLCAKHNMV VANCTTPANF FHILRRQLKW PFRKPLVVFT PKSLLRHPLC VSTISDFTDK
     NFTEVYDDVN VKATDVSRVI FCTGKVYYDL IQHRTEEKIN DTAIIRIEQL YPFPQETVES
     LIKKYKNADE LIWLQEEPDN MGAWAFIQRM MPDAGFKLLS RPEGASPATG SHETHNKEQS
     QLIKSAFERV TA
//