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Database: UniProt
Entry: N8V9Y4_9GAMM
LinkDB: N8V9Y4_9GAMM
Original site: N8V9Y4_9GAMM 
ID   N8V9Y4_9GAMM            Unreviewed;       939 AA.
AC   N8V9Y4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=F975_02233 {ECO:0000313|EMBL:ENU79897.1};
OS   Acinetobacter sp. ANC 3789.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217714 {ECO:0000313|EMBL:ENU79897.1, ECO:0000313|Proteomes:UP000018452};
RN   [1] {ECO:0000313|EMBL:ENU79897.1, ECO:0000313|Proteomes:UP000018452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3789 {ECO:0000313|EMBL:ENU79897.1,
RC   ECO:0000313|Proteomes:UP000018452};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. ANC 3789.";
RL   Submitted (FEB-2013) 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   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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:ENU79897.1}.
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DR   EMBL; APOY01000017; ENU79897.1; -; Genomic_DNA.
DR   RefSeq; WP_004753550.1; NZ_KB851219.1.
DR   AlphaFoldDB; N8V9Y4; -.
DR   PATRIC; fig|1217714.3.peg.2198; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000018452; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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   3: Inferred from homology;
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   939 AA;  104988 MW;  21EF539EE2BF3A9D CRC64;
     MQEVADALRL DTELSADSAA YIEELYEQYL TSPSSVSEDW RQYFDKFPKG DQPHGTVREQ
     FLLLGRNSNR VQSVVQSTVS TEHEKRQIGV LQLISAYRNR GHQKAKLDPL GLAKREDVPD
     LELNAHGLTK SDLDTVFNTG NLAIGKDEAT LGEMVETMQS IYCGSIGAEY MHIVDTVEKR
     WIQQRLEGAR GQFSFTAEQK KHFLERLTAA EGLEKYLGNK FVGAKRFGLE GGETFIPMVN
     EIIQRAGTVG CKEVVIGMPH RGRLNLLVNI MGKNPADLFG EFEGKALTKK GSGDVKYHQG
     FSSNVMTPGG EVHLALAFNP SHLEIVGPVV EGSVRARQVR RKDIGGDDVL PVIVHGDAAF
     AGQGVNMETF QMSQTRGYTV GGTVHIVVNN QVGFTTSDPR DARSTEYCTD IAKMVQSPIF
     HVNGDDPEAV VFIAQLAHDF RHTFRKDVVI DLFCYRRRGH NEADEPSATQ PVMYQVINKK
     ATTRTLYADQ LVQQKILDRA EADKMVEDYR ADLEAGKHVA NALVLEPNTK MFVDWTPYLG
     HDYTDNWDTS FDIERLKAIG TKMRQLPEGF EMQRQVSKVI DERLKMQTGE TPLNWGAAET
     LAYATLLDEG YLVRISGEDV GRGTFSHRHA KLHNQKDGSV YIPLCNVKEN QPRFALWDSL
     LSEEAVLAFE YGYATTLPNS LIVWEAQFGD FANCAQVVID QFIASGETKW ERVCGLTMLL
     PHGFEGQGPE HSSARLERYL QLCAEDNMQV ITPTTPAQIY HALRRQAVRP IRKPLIVMSP
     KSLLRHKLAV SNLDELANGQ FQTVIDEVDQ INKADVTRIV FCGGKVYYDL LEKRREAALG
     NVAIVRVEQL YPYPEQRIAE VLNAYPDATE VVWCQEEPKN QGAWHFIAPF LYETVSNVGK
     QARISFAGRD ASAAPACGSP YLHAKQQAKL IQDALAIEA
//
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