ID   A0A081PED5_9SPHI        Unreviewed;       931 AA.
AC   A0A081PED5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=N180_18105 {ECO:0000313|EMBL:KEQ29058.1};
OS   Pedobacter antarcticus 4BY.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ29058.1, ECO:0000313|Proteomes:UP000028007};
RN   [1] {ECO:0000313|EMBL:KEQ29058.1, ECO:0000313|Proteomes:UP000028007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4BY {ECO:0000313|EMBL:KEQ29058.1,
RC   ECO:0000313|Proteomes:UP000028007};
RA   Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA   Reddy G., Bhargava P.M.;
RT   "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT   Soils of Schirmacher Oasis, Antarctica.";
RL   Int. J. Syst. Bacteriol. 42:102-106(1992).
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:KEQ29058.1}.
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DR   EMBL; JNFF01000085; KEQ29058.1; -; Genomic_DNA.
DR   RefSeq; WP_037442835.1; NZ_JNFF01000085.1.
DR   AlphaFoldDB; A0A081PED5; -.
DR   eggNOG; COG0567; Bacteria.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000028007; 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:UP000028007};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          572..765
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   931 AA;  105056 MW;  CEC6D2D5AC8C48B9 CRC64;
     MDNLSYLNGA NAEYIDSIYQ AYKENPAAVE FGWQKFFEGF DFGRSSEAGV TSEAAPEHFL
     KEVNVLNLIN GYRQRGHLFT KTNPVRERRH HLPTLDIENF GLSKTDLDTV FNSGVELGIG
     AAKLSAIVAF LEKTYCGSVG AEYKFVRTPE VLNWIEQKME RVQNTPNFSI EEKRRILKKL
     NEAVSFENFL GTKFLGQKRF SLEGAESLIP ALDSVIEKGA ELGIEEFVIG MAHRGRLNVL
     ANIMQKTYQD IFAEFEGKGY SAESPFGGDV KYHLGYSTDV TTNDGKSVHL SLCPNPSHLE
     TVNGVVEGMT RSKIDFKYDG DNARIAPILI HGDASVAGQG IVYEVIQMAG LDGYKTGGTI
     HLVINNQIGF TTNYKDARTS TYCTDIAKVT LSPVFHVNGD DPEALVYAIN LAMEYRQKYK
     NDVFIDILCY RRFGHNESDE PKFTQPLLYK TIEKHANPRD IYVQQLISEG KLEAGMAKEM
     EVEFRGILQQ RLNEAKEIVS TYKAVKFAGA WSDMRIASAD DFLVSPDTAV DKSVLLDIAK
     KISTLPAGKK FFKKIEKLFG ERNKMATSTH IFDWAMGEQM AYATLLEEGK RVRLSGQDVE
     RGTFSHRHAV LTLEDSEEEY IPLANLDEKQ ASFDIYNSHL SEYGVLGFEY GYAMANPNAL
     TIWEAQFGDF FNGAQIVVDQ YIASAETKWQ RENGLVMLLP HGYEGQGPEH SSARIERFME
     LCADYNMQVT NCTTPANFFH AIRRQFSRDF RKPLIVFTPK SLLRHPLCVS PLEDFTNGKF
     KEVINDANVK ADDVKRVLYC SGKIYYELLE KQQKEGIKDV AIVRVEQLYP TPLGQMEEIF
     KGYKNANDAV WVQEEPENMG AWPYLLRKTR KTAFNDIEVI SRKESSSTAT GYAKQHADQQ
     AYILAKAFEL PVSSEDKKIA KKSVSKVYNV D
//