ID   A0A495EBU4_9FLAO        Unreviewed;       932 AA.
AC   A0A495EBU4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=CLV91_0244 {ECO:0000313|EMBL:RKR14171.1};
OS   Maribacter vaceletii.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1206816 {ECO:0000313|EMBL:RKR14171.1, ECO:0000313|Proteomes:UP000269412};
RN   [1] {ECO:0000313|EMBL:RKR14171.1, ECO:0000313|Proteomes:UP000269412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25230 {ECO:0000313|EMBL:RKR14171.1,
RC   ECO:0000313|Proteomes:UP000269412};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) 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:RKR14171.1}.
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DR   EMBL; RBIQ01000007; RKR14171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495EBU4; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000269412; 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:UP000269412};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          586..779
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   932 AA;  105837 MW;  49272C7C3C7CC2B5 CRC64;
     MDKYSFLNAV HTSFFAELYD KYLVSPDSVE PSWRAFFQGF DFGMESSIDE LDIAPSSGAI
     IDANGQKIEV PESLQKEFQI IGLIDGYRTR GHLFTETNPV RERRKYTPSL DIENFGLSEN
     DLDTVFSAGE IIGIGPSSLR EIIKNLKSIY CDSIGVEYMY IRNPERVKWI QDWLNVNDNR
     PKLDADGKKH ILKKLNQAVS FEGFLHTKYV GQKRFSLEGN ESLIPGLDAI VERAAEMGVE
     QFVMGMAHRG RLNVLTNIFG KSAKDIFSEF DGKDYEEEIF DGDVKYHLGW TSDRMSDNGN
     KIKMNIAPNP SHLETVGAVV EGIARAKQDA HYKDNFSKVL PIVVHGDAAI AGQGLVYEVV
     QMATLDGYKT GGTIHVVVNN QIGFTTNYLD ARSSTYCTDV GKVTLSPVLH VNADDPEAVV
     HSFLFALEYR MRFSRDVFID LLGYRKYGHN EGDEPRFTQP KLYKAIAKHK NPRDIYAAKL
     IAEGVIGADY VKELENEYKA SLEEELVDSR KEDKTVITPF MADEWSGFEN VREWEMMKPI
     DTTFSTKDLT EIAKVITELP SDKKFLRKVE KLIRDRKKMF FESNKLDWAM GELLAYGSLL
     KEGYDVRMSG QDVERGTFSH RHAVMKVEES EEEVLLLNAI GGDQGKFQIY NSLLSEYGVV
     GFDYGYAMAS PNTLTIWEAQ FGDFSNGAQI MLDQYISAAE DKWKLQNGLV MLLPHGYEGQ
     GAEHSSARME RYLQLCARDN MYIADVSTPA QMFHIMRRQM KANFRKPLII FTPKSLLRHP
     KAVSTVEEFV EGGFQEVIDD TTVSVAKVKS VVFCTGKFYY DLLAVKEADS REDVALVRVE
     QLFPLPADQM KAIISKYKNA DDFVWAQEEP RNMGAWSHMM MHFSDAHKLR VASRRFYAAP
     AAGSAVRSKM RHQQVIDYVF DKTKDNLTRQ KK
//