ID   B5JTK4_9GAMM            Unreviewed;       941 AA.
AC   B5JTK4;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:EDY87332.1};
GN   ORFNames=GP5015_2511 {ECO:0000313|EMBL:EDY87332.1};
OS   gamma proteobacterium HTCC5015.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY87332.1, ECO:0000313|Proteomes:UP000004692};
RN   [1] {ECO:0000313|Proteomes:UP000004692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692};
RX   PubMed=20472792; DOI=10.1128/JB.00510-10;
RA   Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequence of the novel marine member of the Gammaproteobacteria
RT   strain HTCC5015.";
RL   J. Bacteriol. 192:3838-3839(2010).
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; DS990599; EDY87332.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5JTK4; -.
DR   STRING; 391615.GP5015_2511; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000004692; 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:EDY87332.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004692};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          596..789
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   941 AA;  106296 MW;  493B4CD15D72CD19 CRC64;
     MQSLWDSSEF DGANSAYLEV LYENWLEDPD SVAPKWADHF QKIAGKEAKE TEVRHSAVRK
     EFREIARVKD QYIPSTAGDS RKLEHERKQV RVLDLIEAFR SRGHLHAELD PLGRKMPQEV
     PDLSLKHHGL SLSDLDTVFD TGNLFGQTKT SLADILEVLN ETYCGPIGSE VSHVVDSEER
     RWLQQRLESS RGQPNYSGEF KKYILERMTA AEGLERYLHT KYVGQKRFSL EGGEALIPML
     DLLVQDAGRM GMKETVIGMA HRGRLNVLVN IMGKNPADLF QEFEGHLATE SRSGDVKYHM
     GFSSDIKTDG GTAHLALAFN PSHLEIVAPV VEGSVRARQD RRGDGSGSAV LPINIHGDAA
     FAGQGVVMET FNMSQSRGFS TKGTVHIVIN NQIGFTTSNQ KDTRSTYYCT DVAKMVNAPI
     FHVNGDNPEA VCFVTQLALE YRTKFKKDVV IDLICYRRHG HNEADEPSAT QPRMYSRIKA
     LETTRTLYAK HLIGEGVITE EEDREFVDGY RDKLDRGECA QPIIADASED KDLYEVDWEP
     FLGKDWDEPC DTRVDLNTIK SLNEKLLDVP EGHVLHSRVQ KILEDRRKMG SGAMALDWGF
     AETMAYATLV TSWYPVRLTG QDSGRGTFFH RHAVLHHQEK GTAYVPLRHL AKEQANFLVI
     DSLLSEEAVL AFEYGYATSD PHSLVIWEAQ FGDFANGAQV VIDQFISSGE QKWGRLCGLT
     MLLPHGYEGQ GPEHSSARLE RFLQLCAEHN IQVCYPTTPS QIFHLLRRQA IRPCRKPLIV
     MTPKSLLRHK RAVSSLDDLA EGAFMPILGD SVLKTDPNQV KRIVFCSGKI FYDLLEYRES
     EQIEDVAIVR IEQLYPFPEA LLRYEVDRYF NAEEFVWCQE EPMNQGAWYS IQHHIRAMLD
     GEYLHYAGRS ASASPAVGSA KVHVQQQKQL VQDAFSDIPN N
//