ID   V9R8C0_9RICK            Unreviewed;       912 AA.
AC   V9R8C0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   Name=sucA {ECO:0000313|EMBL:AHC39076.1};
GN   ORFNames=EMUR_01300 {ECO:0000313|EMBL:AHC39076.1};
OS   Ehrlichia muris AS145.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=1423892 {ECO:0000313|EMBL:AHC39076.1, ECO:0000313|Proteomes:UP000018689};
RN   [1] {ECO:0000313|EMBL:AHC39076.1, ECO:0000313|Proteomes:UP000018689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS154 {ECO:0000313|Proteomes:UP000018689};
RX   PubMed=24482514;
RA   Thirumalapura N.R., Qin X., Kuriakose J.A., Walker D.H.;
RT   "Complete Genome Sequence of Ehrlichia muris Strain AS145T, a Model
RT   Monocytotropic Ehrlichia Strain.";
RL   Genome Announc. 2:e01234-13(2014).
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; CP006917; AHC39076.1; -; Genomic_DNA.
DR   RefSeq; WP_024071887.1; NC_023063.1.
DR   AlphaFoldDB; V9R8C0; -.
DR   STRING; 1423892.EMUR_01300; -.
DR   KEGG; emr:EMUR_01300; -.
DR   PATRIC; fig|1423892.3.peg.269; -.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000018689; 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   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   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AHC39076.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          569..762
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   912 AA;  103353 MW;  0D2485EEA49C34F0 CRC64;
     MKNVTCLFGD NLDVIEDIYK RYQKDSNSVS LEWRNFFSNG LYSSESIDVV NQSNSVNVID
     SYNAKVVELL NFFRSYGHTV ADLDPLKLHV TGDLDYNKYI DLNDIKPSST FCSVLGLNNP
     TIGDIINALK SIYCNKLGYE FMHIRNHEER MWLQNKIEGF YSSVSNDDKK KILHHLMEVE
     CFEQFLHTKY PGYKRFSIEG GDSLVVAIEK IIDLSTVFNF REIVIGMSHR GRLSVLTKIM
     KKPYKAMMYE FKGGTAYPKD VDVSGDVKYH LGYSSDRQLS PDKTVHLSLC PNPSHLESVD
     PVVMGKIRAK QDVLKECDKS SILGVLVHGD SSVIGQGVVA ETLTLSNLEG YEVRGVIHII
     VNNQIGFTTN PKDSRSSFYC SDVTKLIDAP VFHVNGDSPE DILTAINLAV EYRQKFNKDV
     VIDIVCYRRY GHNEGDEPLF TQPIMYDRVM KHKTPMKLYK EQLINENVIT EEEFKILQAR
     FNSILNEEFA QSESYVPDQA DWLKGNWANF RRPAPGNFVD YLSDTGVDEQ NLLKLARALI
     DIPKEFNGNK KILRILSTRF DMVSSGKDID WATGEALAFA SLLSENVKVR LSGQDCGRGT
     FSHRHAVLID QITGNSYVPL NNLGVPQANF EVINSPLSEY AVMGFEYGYS TDSPSTLILW
     EGQFGDFANG AQIIIDQFIS SAETKWLRCS GLVLLLPHGY EGQGPEHSSA RIERYLQLCA
     EDNMQVVNCT TPANYFHVLR RQMCRDFRKP LVVFTPKSLL RHKMAVSKLS DFSGSFVPVI
     GEVSSLCSSD KIRKVVICSG KVYFDIIEAR DQRKVDDIAV IRLEQYYPFP EEQLASELKN
     YQNAEVVWCQ EEPMNMGAWV FVRNYIEKVL MTINVKSKQT ICISRPASAA TAAGYTSMHN
     REQNDILLHV LS
//