ID   A0A015IHK8_RHIIW        Unreviewed;       956 AA.
AC   A0A015IHK8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Alpha-ketoglutarate dehydrogenase KGD1 {ECO:0000313|EMBL:EXX56637.1};
GN   ORFNames=RirG_214360 {ECO:0000313|EMBL:EXX56637.1};
OS   Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX56637.1, ECO:0000313|Proteomes:UP000022910};
RN   [1] {ECO:0000313|EMBL:EXX56637.1, ECO:0000313|Proteomes:UP000022910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM197198w {ECO:0000313|Proteomes:UP000022910};
RA   Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA   Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA   Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA   Huang S.;
RT   "Single nucleus genome sequencing reveals high similarity among nuclei of
RT   an endomycorrhizal fungus.";
RL   Submitted (FEB-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXX56637.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JEMT01027633; EXX56637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A015IHK8; -.
DR   STRING; 1432141.A0A015IHK8; -.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   OMA; TPAQYYH; -.
DR   Proteomes; UP000022910; 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:UP000022910};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          600..805
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   956 AA;  109275 MW;  21D98F0F03F65E95 CRC64;
     MTNLLNLLSL SNSIIRPINL RIINALSRPI IRPRFNYKIW IQNSKSYHDN EAFGYRVPTT
     EDTMKDYTKV ELSNRIENAN LLRLVTAYRT YGHKEAHLDP LGILEREKVT ALDHERYGFT
     DPNKVYNLNG ILHVNKSAST KVSKEDANIE TILSHLKKVY CGKVAYEFMH IPSASERRWF
     YYTLESYDKT SLTIKEKRKF FELLTRSEVF DHFMSKKFPQ VKRYGLEGAE SMMVALEKLF
     EVSNKAGIIE VVLCMPHRGR LNLLTDLLKF PPVRLFHKVK GNPEFPEHLP ASGDVLSHLA
     SSPILDYGAT NPLSVSMLHN PSHLEAVNPV AMGKTRAKQM DLLKSEKDCK LGDRVMCIQL
     HGDAAFTGQG VVMESFGLSN LPHFTSGGSI HIVVNNQLGY TTPAQNARSS WYSSDIGKMI
     NAPVIHVNGD FPEDVTRAVN VAFEYRNKFG KDVIIDLITY RRWGHNELDE PAYTQPLMYA
     NIRSRKSVPK LYEEKLLAED LIVTQNEMKE FRDNYFKFLE EQYKLSDNHK PEANTLKKKW
     SEMIMPTETV SKLDTGVSRE ILEKVGKISV TVSDDIIIHP RLKKFHIQSR LQRIAEGKNI
     DWATAEALAL GSLLLEGHNV RLCGQDVGRG TFSHRHAMMV CQETERVVVP LNNLSKDQGM
     LEVANSNLSE LAVVGFEYGM SIENPNNLNL WEAQFGDFFN GAQVIIDTYI SSGEVKWLRQ
     SGLVMLLPHG YDGAGPEHSS CRIERFLQLS NDRLDVLNDN IPINPNMHII NPTTPAQYFH
     ALRRQLKRNF RKPLIIMTPK ILLRSPAAVS NFEEMISGTT FLPVLGNDNI LEKSKIEKVV
     FVCGKLYYDL VKERQNKRLE NKVAIIRVEE LCPFPRKDIE QELSNYNNVQ EFIWCQEEPQ
     NNGAFTFIEQ RLNQILPNNQ KIKCISRPIS AAPAVGISKW HYIEHLKILD KVFNNI
//