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
//