ID   A0A241WJG3_9GAMM        Unreviewed;       945 AA.
AC   A0A241WJG3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=B9T35_08895 {ECO:0000313|EMBL:OTG93919.1};
OS   Acinetobacter sp. ANC 3832.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977874 {ECO:0000313|EMBL:OTG93919.1, ECO:0000313|Proteomes:UP000194704};
RN   [1] {ECO:0000313|EMBL:OTG93919.1, ECO:0000313|Proteomes:UP000194704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3832 {ECO:0000313|EMBL:OTG93919.1,
RC   ECO:0000313|Proteomes:UP000194704};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
RL   Submitted (APR-2017) 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};
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:OTG93919.1}.
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DR   EMBL; NEGJ01000005; OTG93919.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A241WJG3; -.
DR   STRING; 1977874.B9T35_08895; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000194704; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          593..786
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   945 AA;  105557 MW;  F5C63097E9D00E0F CRC64;
     MQEVADAMRL DTELSADSAA YIEELYEQYL SSPTSVGDDW RAYFDKFPKG DQPHGNIREQ
     FLLLGRNSSR VQPVVQSEVS TEHERRQIGV LQLIAAYRNR GHQKAKLDPL GLAKREDVPD
     LDLSTHGLTK SDLDTVFNAG NLAIGKTEAT LGEMVNAMEA TYCASVGVEY MHIVDTKEKR
     WIQQRLESTR GQFGYSAEQK KSVLERLTAA EGLEKFLGNK YVGAKRFGVE GGESFIPMVN
     ELIQRAGAVG CKEVVIGMPH RGRLNLLVNI MGKNPADLFG EFEGKSIHKK GSGDVKYHQG
     FSSNVMTPGG EVHLALAFNP SHLEIVGPVV EGSVRARQVR RKDIGGDDVL PIIVHGDAAF
     AGQGVNQETF QMSQTRGYTV GGTVHIVVNN QVGFTTSDPR DARSTEYCTD IAKMIQAPIF
     HVNGDDPESV LFVTQLAHDF RHTFRKDVVI DMFCYRRRGH NEADEPAATQ PMMYQVISKK
     ATTRTLYADQ LVQQNIVDRA AADQMVEDYR SDLEAGKHVA NALVLEPNDK MFVDWKPYLG
     HDYTDVWDTT FPIERLKELG TKMRELPEGF VMQRQVSKVI DDRLKMQTGE MPLNWGAAEV
     LAYATILDDG YLVRLTGEDV GRGTFSHRHA KLHNQVDGSV YIPLCHIKEN QPRTAIYDSL
     LSEMAVLAFE YGYATTLPKS LVIWEAQFGD FANCAQVVID QFIASGETKW ERVCGLTMLL
     PHGFEGQGPE HSSARLERFL QLCAEDNMQV ITPTTPAQIF HAMRRQAIRP IRKPMIVTSP
     KSLLRHKLAT STLEELATGT FQTVIDEVDQ INKADVTRLV LCGGKVYYDL LEKRREQNLN
     IAIVRVEQLY PFPEQRIAEV LATYPNVQEI VWCQEEPKNQ GAWLFIAPRL YEGVMKSGKQ
     VRISYAGRDA SAAPACGSPY LHAKQQAQLV NDALAIVADQ SGETK
//