ID   I1C2A2_RHIO9            Unreviewed;       728 AA.
AC   I1C2A2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component {ECO:0000313|EMBL:EIE82582.1};
GN   ORFNames=RO3G_07287 {ECO:0000313|EMBL:EIE82582.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE82582.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE82582.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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; CH476736; EIE82582.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1C2A2; -.
DR   STRING; 246409.I1C2A2; -.
DR   VEuPathDB; FungiDB:RO3G_07287; -.
DR   eggNOG; KOG0451; Eukaryota.
DR   InParanoid; I1C2A2; -.
DR   OMA; TPAQYYH; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000009138; 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; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
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; 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:UP000009138};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          579..728
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   728 AA;  82296 MW;  4AAE8A15EF7B16A7 CRC64;
     MLRAISCNII KKPKGHSLLK TRSYHDDGVF GYRVPKEFKL PDYTEQELAN RMKHGGLLRM
     VQAYRTHGHE GAQLDPLDIM KRKEVLALKP ERYGLEKQDD RYNLAGILHV NDAMQSNTSG
     GEEADFKTIL NHLQAVYCGK IAYEFMHLPS ASERRWWYHA VESWQKPELT VTQKKRIHEM
     LVKSEVFDQF LAKKFPNVKR YGLEGAESMM VALDRLFELS AVNGVQDIVI GMPHRGRLNL
     LCDLLEYPHA ALFHKMKGRS ELPEGTFASG DVISHLTNNP NLDYHGKKVH VSLLHNPSHL
     EAINPVAMGK ARAKQTELLA SAESSCNLGD RVMCIQIHGD AAFTGQGVVM ESFGLSNLPH
     YSSGGSVHIV VNNQLGYTTP AQNARSSAYC SDIGKMINVP IVHVNGDYPE DVAKALDVVF
     EYRNKFRKDI ILDLMCYRRW GHNELDEPAF TQPQMYNNIR HRTSVPKSYE KKLVQESVFA
     TENEPEAVRK RYSDELEQGL KQAESYKTSS DYHLQGNWKG LEHIKVHSSE QVETGCDLEL
     LKKVGQASVS APDDIKIHSR LQKYHIDQRL KKIAQGHSLD WATAEALAFG SLLKQDMDVR
     ISGQDVGRGT FSQRHAMFVC QETERTIIPL NHMNNKHYLE VANSPLSEFA VLGFEYGMSL
     ESPNRLVLWE AQFGDFFNGA QIIIDTFLSS GESKWLRQSG LVMLLPHGQD GAGPEHSSSR
     VERFLQAN
//