ID   A0A1A7RDX9_9GAMM        Unreviewed;       940 AA.
AC   A0A1A7RDX9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, 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=A9J31_12385 {ECO:0000313|EMBL:OBX29729.1};
OS   Acinetobacter gandensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1443941 {ECO:0000313|EMBL:OBX29729.1, ECO:0000313|Proteomes:UP000185753};
RN   [1] {ECO:0000313|EMBL:OBX29729.1, ECO:0000313|Proteomes:UP000185753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4275 {ECO:0000313|EMBL:OBX29729.1,
RC   ECO:0000313|Proteomes:UP000185753};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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};
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:OBX29729.1}.
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DR   EMBL; LZDS01000004; OBX29729.1; -; Genomic_DNA.
DR   RefSeq; WP_067762463.1; NZ_VZOF01000009.1.
DR   AlphaFoldDB; A0A1A7RDX9; -.
DR   STRING; 1443941.A9J31_12385; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000185753; 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   940 AA;  104880 MW;  15515633F334A1CB CRC64;
     MQEVADALRL DTELSADSAA YIEELYEQYL TAPDSVEADW RAYFDKFPKG DQPHSNVREQ
     FLLLGRNSSR VQPVVQSAVS SEHERRQIGV LQLIAAYRNR GHQNAKLDPL GLAKREIVPD
     LDLAAHGLTQ SDLDTVFNTG NLAIGKSEAT LGEMVQAMEA TYTASIGVEY MHIVDTKEKR
     WIQQRLEGAR GQFGFSAEQK KHVLERLTAA EGLEKYLGNK FVGAKRFGVE GGESFIPMVN
     ELIQRAGSVG CKEVVIGMPH RGRLNLLVNI MGKNPADLFG EFEGKALHKK GSGDVKYHQG
     FSSNVMTPGG EVHLALAFNP SHLEIVGPVV EGSVRARQVR RKDIGGDDVL PIIVHGDAAF
     AGQGVNQETF QMSQTRGYTV GGTVHIVVNN QVGFTTSDPR DARSTEYCTD IAKMIQAPIF
     HVNGDDPESV LFVSQLAHDF RHTFRKDVVI DMFCYRRRGH NEADEPAATQ PMMYQVINKK
     ATTRTLYADQ LVQEGVLDRA AADAMVEQYR SDLEAGKHVA NALVLEPNTK MFVDWKPYLG
     HEYTDKWDTT FPIERLKELG AKMRELPEGF VMQRQVAKVI DDRLKMQTGE MPLNWGAAET
     LAYASILDEG FLVRLTGEDV GRGTFSHRHA KLHNQVDGST YIPLCNLKEN QPRTAIYDSL
     LSEMAVLAFE YGYATTLPKS LVIWEAQFGD FANCAQVVID QFIASGETKW ERVCGLTMLL
     PHGFEGQGPE HSSARLERFL QLCAEENMQV ITPTTPAQIY HAMRRQALRP IRKPMIVTSP
     KSLLRHKLAT STLEELANGT FQTVIDEIDN INKSDVTRLV LCGGKVYYDL LEKRREKELN
     NTAIVRIEQL YPYPEARLAE VLAQYPNVTE LVWAQEEPKN QGAWLFIAPR LYDDVMKAGK
     QVRISYAGRE ASAAPACGSP YLHAKQQAQL VNDALAIVAE
//