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Database: UniProt
Entry: A0A3G2L2S1_9FLAO
LinkDB: A0A3G2L2S1_9FLAO
Original site: A0A3G2L2S1_9FLAO 
ID   A0A3G2L2S1_9FLAO        Unreviewed;       940 AA.
AC   A0A3G2L2S1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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=D1013_03635 {ECO:0000313|EMBL:AYN66538.1};
OS   Euzebyella marina.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Euzebyella.
OX   NCBI_TaxID=1761453 {ECO:0000313|EMBL:AYN66538.1, ECO:0000313|Proteomes:UP000276309};
RN   [1] {ECO:0000313|EMBL:AYN66538.1, ECO:0000313|Proteomes:UP000276309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN62 {ECO:0000313|EMBL:AYN66538.1,
RC   ECO:0000313|Proteomes:UP000276309};
RA   Xue C.;
RT   "The reduced genetic potential of extracellular carbohydrate catabolism in
RT   Euzebyella marina RN62, a Flavobacteriia bacterium isolated from the hadal
RT   water.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP032050; AYN66538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G2L2S1; -.
DR   KEGG; emar:D1013_03635; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000276309; Chromosome.
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:AYN66538.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276309};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          586..779
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          921..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   940 AA;  107485 MW;  1BD7416E0D083104 CRC64;
     MDKYSFLNAA HTAFFADLYD KYLKAPDSVE PSWRAFFQGF DFGSELALED FDVSELVNGS
     VSQNGQAVEV PNSLQKEFQV IRLIDGYRSR GHLFTKTNPV RERRKYEPTL EIENFGLSQS
     DMSTVFNAGE IIGIGASTLA DIIDHLQRIY CDAIGVEYMY IRNPERIEWI QQWLNVNDNH
     PKFDVEHKKR ILKKLNQAVS FEGFLHTKYV GQKRFSLEGN ESLIPALDAV VERAAELGVE
     QFVMGMAHRG RLNVLTNIFG KAAKDIFSEF DGKDYEQEIF DGDVKYHLGW TSERKTDNGR
     RIKMNIAPNP SHLETVGAVV EGITRAKQDT HFPEDFSKVL PIVVHGDAAI AGQGLVYEVV
     QMATLDGYKT NGTIHIVVNN QIGFTTNYLD ARTSTYCTDV GKVTLSPVLH VNADDAEAVV
     HASLFALEYR MRYNRDVFLD LLGYRKYGHN EGDEPRFTQP KLYKAIAKHS NPRDIYAEKL
     IQEGVIEEGY VKKLEEEYKA SLEEELEDSR KEDKTKITPF MADEWKGFSN VREWEMMDKV
     DTSFEESKLT EIAKVITELP EGKKFLRKVE KLVRDRKKMY FETQTLDWAM GELLAYGTLL
     SEGYGVRMSG QDVERGTFSH RHAVMKVEES EEEVMLLNHI SEDQGKFQIY NSLLSEYGVV
     GFDYGYAMAS PNTLTIWEAQ FGDFSNGAQI MIDQYISAAE DKWKLQNGLV MLLPHGYEGQ
     GAEHSSARME RYLQLCARDN MYIADVSTPA QMFHILRRQM KVNFRKPLII FTPKSLLRHP
     KAVSSVDELA NGSFQEVIDD TNVKAKEVKT LVFCTGKFYY DLLAAKEEHS RNDVALVRVE
     QLFPLPTEQM KEIISKYENA DDIVWAQEEP RNMGAWSHLM MHFPESQQFR VASRRFYASP
     AAGSAVRSKM RHQQVIDYVF DKSKDNMSKP TPKPKEEAKA
//
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