ID A0A2H3EF43_ARMGA Unreviewed; 935 AA.
AC A0A2H3EF43;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=2-oxoglutarate dehydrogenase, E1 component {ECO:0000313|EMBL:PBK98993.1};
GN ORFNames=ARMGADRAFT_1051258 {ECO:0000313|EMBL:PBK98993.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK98993.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293647; PBK98993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3EF43; -.
DR STRING; 47427.A0A2H3EF43; -.
DR InParanoid; A0A2H3EF43; -.
DR OMA; TPAQYYH; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000217790; 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:UP000217790};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 576..780
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 935 AA; 105070 MW; D9E4D2ADCCD7C2B3 CRC64;
MHSLRRLRLQ QKSSLCRLYH DESFGYRKPR PFVFPDYTPA QLENRAHNAA LLRYVDSVRT
HGHRAARIDP LDLIHRKEVA ALDPSRYGLT DESKKYNVNG IIWTHPSVES QGENMTEEWW
SLGEIVRHLR SIYVNRIAYE YMHSPSKSER LWFSHRLESK STPTTLDADT KRRIHGLLAR
SEVFDNFMQV KFPNLKRYGL EGGESMLPAL DSLFSSAAQA DVSHIVLAMP HRGRLNLLTD
LLNYNPTALF HKVRGGAEIP EDLGAEGDVI SHLVSSTVLN YDSDNQAVKV SLLPNPSHLE
AVAGVALGKA RAKQYSLLKT SAEDCKLGDK VMCVQLHGDA SFTGQGVVME SLGLSNLPHF
TSGGTVHLVV DNNIGYTTPA SQARSSLYCS DIGKMINTPV LHVNGDYPED VVKAMEVAFQ
YRQYFRKDII VDLLVYRRWY HNELDLPNLT SPLMYDKIQS RLSVPQLYEQ KLVNERTLTT
EDIANVREQY KSNLNDKLDK VPSYVPSASM LQEQWAGMVW PISKSAVQSP DTGVDTDILI
RVGKASVQVP QGFEIHPKLQ RHIKNRLASL ESGKGLDWAT AEALAFGSLL LEGYDVRISG
QDVGRGTFSQ RHAMLVNQKD ENTVVPLNDE LSALGKLELA NSSLSEMAVL SFEYGASWER
PDLLPIWEAQ FGDFFNGAQI IIDTFISSSE SKWLKQSGIV MLLPHGLDGA GPEHSSSRIE
RMLQLTNDRY TYEEDPSFNI NMHVVFPTTP AQYFHLLRRQ MKRNYRKPLI VAGPKGLLRL
SPAASSLSDL ETGTSFRPVL ADPYDNAATA SRVIILSGKI YYDLLKERQA RGLDANIALV
RLEELSPFPF AELATVLEGY TSAREFFYLQ EEPRNQGAFG HVKERIMWVL KEMVGAGDVE
LVYKGRKESQ LPAPGIGKLY QAQQRTVLES AFEGF
//
