ID   A0A1H0J9V6_9GAMM        Unreviewed;       963 AA.
AC   A0A1H0J9V6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=SAMN04487951_12511 {ECO:0000313|EMBL:SDO40507.1};
OS   Halomonas arcis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=416873 {ECO:0000313|EMBL:SDO40507.1, ECO:0000313|Proteomes:UP000199677};
RN   [1] {ECO:0000313|Proteomes:UP000199677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6494 {ECO:0000313|Proteomes:UP000199677};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNII01000025; SDO40507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0J9V6; -.
DR   STRING; 416873.SAMN04487951_12511; -.
DR   Proteomes; UP000199677; 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:UP000199677};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          617..810
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  107987 MW;  67115CCA61CFA650 CRC64;
     MSPRARDDTD TTPSVQGDRE MQQGIMELMW RSSHVSGGNA HYVEALYEQY LDDSESVPDE
     WRSYFDQLPR PEGSATHDVP LSPIRDQFYQ LGRENRPRVA AAAESGENKK QVKVLQLINA
     YRFRGHQKAN IDPLGLRNPT PVPDLDLSFH QLSKADLDSE FQTGSFFLGI DKAPLRVIVD
     ALERTYCRSI GCEIMHIVDT EEKRWLQRRF ESVRSAPEFS DGVRKHVLER LTAAEGLENY
     LASKYPGTKR FGLEGGEAFV PMMDELIQRA GGYGTKEVVI GMAHRGRLNL LVNILGKNPT
     DLIDEFDGKK VIERGSGDVK YHQGFSSNVM SPGGEVHLAM SFNPSHLEIV APVVEGSVRA
     RQDRRNDEEG SKVLPINVHG DAAFAGQGVV METFQMSQTR AYKTGGTVHI VINNQVGFTT
     SHPLDARSTE YCTDIAKMVQ APIFHVNGDD ADAVLHATQV ALDYRQEFKK DVVIDLVCYR
     RRGHNEADEP SGTQPMMYSK IKDHPSSRSL YAKRLVDQGV LSEEDAKAMI ETYRDDLVAG
     NHVANALVQE PNTSLFVDWT PYLGHEWTGN ADTTFDMKRL QQLAAKMCEV PDGIDVQRQV
     AKIYEDRRKM QAGGMGLNWG FAETLAYATL LDQGHPIRIT GQDVGRGTFS HRHAVVHNQK
     DGSTYVPLQN MSDGQPRFTI HDSILSEEAV LAFEYGYSTT APSGLVVWEA QFGDFFNGAQ
     VVVDQFISSG ETKWGRLCGL TMLLPHGYEG QGPEHSSARL ERFLQMCAEH NMQVCVPTTP
     AQIYHLLRRQ VIRPLRKPLV IMSPKSLLRH KEAVSSLEDL AHGKFHMVLS DQSDLAAEKV
     TRAILCAGKV YYDLAAWRAE NERHDTAILR LEQLYPFPKE ELLEALQAYT QLEDIVWCQE
     EPLNQGAWYS SQHHMRTVAD MLKDGLGREL KFAGRPASAA PAAGYMSVHT EQQRQLVEDA
     FNL
//