ID Q7VR91_BLOFL Unreviewed; 970 AA.
AC Q7VR91;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=sucA {ECO:0000313|EMBL:CAD83398.1};
GN OrderedLocusNames=Bfl331 {ECO:0000313|EMBL:CAD83398.1};
OS Blochmannia floridanus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=203907 {ECO:0000313|EMBL:CAD83398.1, ECO:0000313|Proteomes:UP000002192};
RN [1] {ECO:0000313|EMBL:CAD83398.1, ECO:0000313|Proteomes:UP000002192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kramerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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};
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DR EMBL; BX248583; CAD83398.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7VR91; -.
DR STRING; 203907.Bfl331; -.
DR KEGG; bfl:Bfl331; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000002192; 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: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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAD83398.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 621..816
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 970 AA; 112644 MW; 2714415E57AAF351 CRC64;
MNSDIFKAWL NSSFLTKNNQ SYIDQIYEFF LKNPHSIDIS WINIFKEWDI EEKNQNQSII
NKQLHSTSPL LSEYDKQDNS YKSYISTDID KEKTINISKI LQLIHSFRKY GHQYSILDPL
GLTINTVKNS FLELKYYKFL DKDVLQQFDT NLLGMNKGII TLNSIYKFLK KTYCGTIGIE
YMHILDINQI LWIQDYFESH TIEISDHFSV KEQRQFLNEL IASEELERYL GIKFPGSKRF
SLEGGDVLIP MLKEAIRYSV LNHNIQEIFL GMPHRGRLNT LINVLGKNPQ DLFNEFYGTN
QKYTNSGDVK YHQGLYSEVT INSQIVHISL LFNPSHLEII TPVMMGAARA RIEQLYKDQI
HKTILNKNYK IQQNIVLPIT IHGDAAISAQ GVVQETLNMA NTRAYSVGGT IHIVINNQIG
FTTSNIDDIR STPYCTDIAK MIQAPILHVN ADDVHAVIFV TRFALNFRNK FKHDIVIDLV
CYRRHGHNET DEPHVTQPMM YQKIRNHPTV LELYAQKLIQ KNIINVDDIK NESCLYRSKL
DNENCVLEKN WKPVHVRSKY HVLDINQDTS YIINNSIKID KQSLQQLACN IFNIPNSITM
HDRVKKIYHE RMEMALGNRL FDWGGAEILA YAVLLNQGYS IRLSGEDTAR GTFFHRHAII
YDQKSTKKYI PLMNIKQKQG SFLIWNSVLS EESALAFEYG YAHVASHNTL VIWEAQFGDF
SNGAQVVIDQ FISSGEQKWN QLCGLIMLLP HGYEGQGPEH SSCRIERYLQ LCSEYNMRIC
IPSTPDQIYH LLHQHAHDKI RRKPLIIVSP KSLLRHPMVH ASIEDFTYGS FKAIISETNN
NCILTQVNKI IICTGKIYYD LVNKRNQLKK YNIAIIRIEQ LYPFPHVDIK IILKPYLHVE
NFIWCQEEPQ NQGAWYYIQL YFHKYIPNIT LNYMGRDEAA APASGYFSQH QQQQTKIINQ
ALDIINNEEG
//
