ID   Q2GDI7_NEOSM            Unreviewed;       905 AA.
AC   Q2GDI7;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   Name=sucA {ECO:0000313|EMBL:ABD46269.1};
GN   OrderedLocusNames=NSE_0578 {ECO:0000313|EMBL:ABD46269.1};
OS   Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia
OS   sennetsu).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=222891 {ECO:0000313|EMBL:ABD46269.1, ECO:0000313|Proteomes:UP000001942};
RN   [1] {ECO:0000313|EMBL:ABD46269.1, ECO:0000313|Proteomes:UP000001942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-367 / Miyayama {ECO:0000313|Proteomes:UP000001942};
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR   EMBL; CP000237; ABD46269.1; -; Genomic_DNA.
DR   RefSeq; WP_011451965.1; NC_007798.1.
DR   AlphaFoldDB; Q2GDI7; -.
DR   STRING; 222891.NSE_0578; -.
DR   KEGG; nse:NSE_0578; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   Proteomes; UP000001942; Chromosome.
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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; 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; 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   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABD46269.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          572..764
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   905 AA;  102254 MW;  C1839DBF6C9D1572 CRC64;
     MKGTRMKVAD DELLKKVHRA YLDSPNSVDP SWRAFFESRG CVKRSGGQSG FSNMSFVRKD
     NGAVRENAVS EQSLLDIKIK DLKDAYRRFG YLAADLDLLG LVKPIVRPEL NPEFHGLSDV
     SLSSGFTVEQ IVCEMHAVYC GHIGVQFMHL SDNSEVTWLE ERLEGRPFCR IGFGTSHKLA
     LLDVLIRVNG LEEFVNTKFR AVKRFSVEGC DTALVALESI IEVAANAGCT DVIVGMSHRG
     RLNSLVNTFG KKYRALFHGF EGKSPFPEEC KIHGDVKYHY GFSCERKTFL SEKTIFARLL
     HNPSHLDSVD PVLVGAARAA KDSGAVVFPV LLHGDAAFSG QGVVYETMLL EELPNYESGG
     VIHIILNNQI GFTTSPQDVR KQRYPSFIGE SFDIPIFHVN GDDPEAVFYV TLLAAEFRNT
     FNKSAIVDIV SYRRHGHNEI DEPRFTQPEM YDVIERHKRS VDIYVERLIK EGVISQDKFV
     ELTQNFGGLL DKELKEAKTY KPSYEGLIQK GWERYLGQEG RDEPQVETKV PKEVLLSLSE
     KLNHIPEGFD VSPKVLRLLV RREETIVSEC DVDWGNGENL AFATILNDGM SVRLAGQDCK
     RGTFSHRHAV LTSQSTGEEL CLLNHISDVA KMQVIATPLS EYAALGFEYG YSLINPKTLV
     LWEAQFGDFA NGAQIIIDQF ISSAESKWLS RSGLVMLLPH GYEGQGAEHS SARIERFLQL
     AADNNMRVAN CTTPANFFHV LRRQVLSEIV RPLVVFTPKS LLRHKMAVSK LEEFYEGSFR
     PVISDYCSDA KKIHRVIFCS GKVYYDLLAE LKSESILLVR VEQLYPVPDR EIREILDVYR
     DAEFIWCQEE PRNMGGWSFM LQVFEERYSK KLRYIGRNYY PVPSEGLMDD HIANQAALIK
     QAITV
//