ID H8K4B8_RICAG Unreviewed; 928 AA.
AC H8K4B8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:AFC69362.1};
GN OrderedLocusNames=MCE_01840 {ECO:0000313|EMBL:AFC69362.1};
OS Rickettsia amblyommatis (strain GAT-30V) (Rickettsia amblyommii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=1105111 {ECO:0000313|EMBL:AFC69362.1, ECO:0000313|Proteomes:UP000008005};
RN [1] {ECO:0000313|Proteomes:UP000008005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAT-30V {ECO:0000313|Proteomes:UP000008005};
RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT "Complete genome sequence of Candidatus Rickettsia amblyommii strain GAT-
RT 30V.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFC69362.1, ECO:0000313|Proteomes:UP000008005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAT-30V {ECO:0000313|EMBL:AFC69362.1,
RC ECO:0000313|Proteomes:UP000008005};
RX PubMed=27638476; DOI=10.1099/ijsem.0.001502;
RA Karpathy S.E., Slater K.S., Goldsmith C.S., Nicholson W.L., Paddock C.D.;
RT "Rickettsia amblyommatis sp. nov., a spotted fever group Rickettsia
RT associated with multiple species of Amblyomma ticks in North, Central and
RT South America.";
RL Int. J. Syst. Evol. Microbiol. 66:5236-5243(2016).
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; CP003334; AFC69362.1; -; Genomic_DNA.
DR RefSeq; WP_014391893.1; NC_017028.1.
DR AlphaFoldDB; H8K4B8; -.
DR STRING; 1105111.MCE_01840; -.
DR KEGG; ram:MCE_01840; -.
DR HOGENOM; CLU_004709_1_0_5; -.
DR Proteomes; UP000008005; 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:AFC69362.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 585..778
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 928 AA; 103792 MW; A641BA35272E98DE CRC64;
MEEDLKKTGY LFGGNAVFVE ELYKQYLANP ASVDQTWQEF FAGIKDNNTL LNKSTAKIII
PDEIKKESLN NNLSSEDLNS LKAKEMINAY RKHAHYLANL DPLGLELRKT KNDLKLNIEA
FGLDSGQLEE NINITDEFVG TWNCKLSELV TKFDKVYTGS IGVEFEQIEN VEGKNWLYNK
LESEVTFSSE DKKTILNDLV EVEGFEQYLH TKFPGAKRFS VEGGDASIVA MSKAIDLSMH
QGVSEIVIGM AHRGRLNTLT KVIGKPYKAV IAGFISGSVF PDELNVSGDV KYHLGYSSDR
TLEDKKIYLS LADNPSHLEA VNPIVAGTVR AKQDILGDTK RSKVKAILVH GDAAFCGQGV
VAESLSMSPL AAYDIGGILH FVINNQLGFT ANAADTRTSR YSTEFAKIIA APILHVNGDD
IEAVLKATNI AVEYRQKFGK DVVVEIICYR KYGHNEGDEP MYTQGKMYNI IKNKLTPGNI
YANELVKSGV IDNNYFAKLK EEFKAKLDKE YEQAKSYKQE AHCLGGLWQG IARTRTQATI
TGISKKTLHD LGTKLCEIPK DFAVNPKLVK LFEARKATLT ADQPIDWATA EQLAFASLLA
SGTNIRLTGQ DSGRGTFSHR HSVLHNQIDD TTYIPLNNLS KEQAKYEVAD SNLSEYAVLG
FEYGYSLANP KNLVLWEAQF GDFANGAQII FDQFISSSET KWLRMSGLVV LLPHAFEGQG
PEHSSARLER FLQLVAENNM YVTYPTTPAS IFHLLRRQIL DDTRKPLIVM SPKSLLRHKY
AVSKLDELGE NTTFLPVLDE VTKVDTNNIT KVILCSGKVY YDLFEMRGNN SNIAIIRLEQ
LYPFEKKLVA SLLKKYNRTQ EFIWCQEEPK NMGTWCYIVS HLNDALKEAG INNEFKYVGR
EESASPAVGS LQAHNKQQEK LLRAALGI
//
