ID   A0A058Z9Q9_FONAL        Unreviewed;       967 AA.
AC   A0A058Z9Q9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component {ECO:0000313|EMBL:KCV70272.1};
GN   ORFNames=H696_02602 {ECO:0000313|EMBL:KCV70272.1};
OS   Fonticula alba (Slime mold).
OC   Eukaryota; Rotosphaerida; Fonticulaceae; Fonticula.
OX   NCBI_TaxID=691883 {ECO:0000313|EMBL:KCV70272.1};
RN   [1] {ECO:0000313|EMBL:KCV70272.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38817 {ECO:0000313|EMBL:KCV70272.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Brown M., Walker B., Young S.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fonticula alba ATCC 38817.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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DR   EMBL; KB932204; KCV70272.1; -; Genomic_DNA.
DR   RefSeq; XP_009494788.1; XM_009496513.1.
DR   AlphaFoldDB; A0A058Z9Q9; -.
DR   STRING; 691883.A0A058Z9Q9; -.
DR   EnsemblProtists; KCV70272; KCV70272; H696_02602.
DR   GeneID; 20527327; -.
DR   eggNOG; KOG0451; Eukaryota.
DR   OMA; TPAQYYH; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000030693; Unassembled WGS sequence.
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; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030693};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          584..800
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..39
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   967 AA;  105300 MW;  31EF09B2456AEBE7 CRC64;
     MGRGRPRRTG GGRGNAGTPP PLPPPPPPPP PPLPPFKTRR PSPTALANRN KYANALRLVE
     AYRTHGHVLS SLNPLAPAAA GQKQDSQAVE TRRLLNPALY GLTLEDTIST EGIVADLPAE
     VTVAELIATL DRTYSASIGY EFTYLPTEAE REWFASAVER LAAAPATDAA TSMRMWERMM
     RSEVFDQFMT KRFAQVKRYG CEGIESMHVG LEAIFEAANR AGVSDIVLGM PHRGRLNLLT
     DLMGLPAEAL FHKLATGESE LPPDAIASGD VLSHIAASVD LAFGGEGSPA THISMLHNPS
     HLEAVNPVTT GKARAKLTMK EAFTPGVTSA QPDLSVLALQ VHGDSAFAGQ GVVPETLLLA
     NIPHYTTYGS VHVVVNNQVG FTTQNRNARS TRYASDVAKS ISAPVIHVNA EDPEAVRAVF
     TLATEYRQTF GRDVVLDLIG FRRWGHNELD EPAFTQPLMY ADVRARESVV TKYERDVILA
     KGHASAEELQ QRRAAYEAVL DAALDRCRSY VPPKEDLAGR WTGIERSPAC RSHETAPVTG
     VPMERLLAAG RASVTVPDTV QPHDRLVRTH LRNRLRRLDA GEPVDWATAE AMAFGTLLAD
     GQVVRLSGQD VGRGTFSHRH AMLVDQTSDE VHVPLNSALL PALEEAGVAG PAPVGRIELA
     NSPLSELAVL GFEYGHSLDT PNTLTLWEAQ FGDFWNTAQV MVDTFTTCSE TKWLRQSSLT
     MLLPHGYDGT GPEHSSSRIE RFLQLSDEPF AKLDGNMPLP NVIIANPTTP AQYFHILRRQ
     QARSFRKPLV LATPKTLLRL PAAVSPLEDL TPASGGFKPV LADPAFADGR AYSAERVLLC
     SGKLYYELVA ERARRGLDDK VAIVRVEELS PFPFDALRET LDQYSNAVNC SNNLVWVQEE
     HQNQGPWTYV QPRINSLYAS EDVMYAGSGE PAGIRYVGRA PLGCPATGIS KVHQAEVAKI
     YEDAFTA
//