ID A0A077FLA2_9RICK Unreviewed; 937 AA.
AC A0A077FLA2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:AIL65300.1};
GN ORFNames=NOVO_04610 {ECO:0000313|EMBL:AIL65300.1};
OS Rickettsiales bacterium Ac37b.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=1528098 {ECO:0000313|EMBL:AIL65300.1, ECO:0000313|Proteomes:UP000028936};
RN [1] {ECO:0000313|EMBL:AIL65300.1, ECO:0000313|Proteomes:UP000028936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac37b {ECO:0000313|EMBL:AIL65300.1,
RC ECO:0000313|Proteomes:UP000028936};
RA Felsheim R.F., Kurtti T.J., Johnson S., Labruna M.B., Munderloh U.G.;
RT "Genome sequence of a novel Rickettsiales species cultured from Amblyomma
RT cajennense.";
RL Submitted (JAN-2015) 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 -!- 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; CP009217; AIL65300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077FLA2; -.
DR STRING; 1528098.NOVO_04610; -.
DR KEGG; rbt:NOVO_04610; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_5; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000028936; 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:AIL65300.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028936};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 592..785
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 937 AA; 106508 MW; 024FC9FA45515821 CRC64;
MYEEKNSYLY PANVSFIEEL YAKYLEDKES VDKTWQDFFA SFPNEQELKA SWTKIDTKVI
LGPEKTPEIK GKAIPVESNN KLQVKALIND YRRLGHFAAD LDPLKLEKTP SINDLGLEAI
NYGFAESDYD QNLPEEIEGL GLVTLRKLES FLQKVYCNHI GTEFLHIENK EEVEWIKNKI
ESLPFEKEFS ADKKKSLLKD IIQVEGFEQF VHSRFPGAKR FSVEGGANSI CVIDEIINKS
TDFDVKEAIL GMAHRGRLNV LTKIVGKPYK HMLAEFSGTK AYPEDLNVDG DVKYHLGASG
DREVNNKKIY LSLTPNPSHL EAVNPVVAGK VRAKQDFCGD KERNKIMGIL IHGDAAFTGQ
GVVAETLVLG ELEGYCTGGT IHVVINNQIG FTTDPKKGRP NRYSTEFAKI IEAPIFHVNG
DDIEALIRIS HIAVEFRQKF KKDVVIDVTC YRLYGHNETD EPAFTQPIMY KNIGKHKTSA
EVYAEKLIEQ KIINVDEFKQ IKEDFFKYLD QELEAAKSYK PKEADWLSGK WQGFERVSDE
GFIDKENTGV DIDKLKSIGK ALTNIPSGFS VNSKISRQLE LKKKMLETGE GIDWSTAESL
AFGTLLSEKI AVRLSGQDSG RGTFSHRHAV LVDQENNSNY IPLNNLNQEQ SNFEVIDSNL
SEYAVLGFEY GYSYVEPKSL VLWEAQFGDF ANGAQIIIDQ FIAAAETKWL RMSGLVMLLP
HGYEGQGPEH SSARLERFLQ LCAEYNLQIA NCSTPASYFH ILRRQIHRKY RKPLIIMSPK
SLLRHKLAIS NLKEFSGDSK FRPLIPEELL NPNDKDIRKV VFSSGKVYYD LLEERNKLGI
NDVALVRLEQ YYPLPKVAII EQLKKYKNAE FVWCQEEPRN MGAWGFLKDK FEELLQELKL
SNKVLLYAGR KEAASPASGY KKTHDQEQET LIKEALN
//
