ID D5GC71_TUBMM Unreviewed; 1044 AA.
AC D5GC71;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 03-MAY-2023, entry version 57.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ82114.1};
GN ORFNames=GSTUM_00000610001 {ECO:0000313|EMBL:CAZ82114.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ82114.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ82114.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ82114.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FN430103; CAZ82114.1; -; Genomic_DNA.
DR RefSeq; XP_002837923.1; XM_002837877.1.
DR AlphaFoldDB; D5GC71; -.
DR STRING; 656061.D5GC71; -.
DR EnsemblFungi; CAZ82114; CAZ82114; GSTUM_00000610001.
DR GeneID; 9184790; -.
DR KEGG; tml:GSTUM_00000610001; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_003662_1_0_1; -.
DR InParanoid; D5GC71; -.
DR OMA; MIVAVNW; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:EnsemblFungi.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:EnsemblFungi.
DR GO; GO:0000103; P:sulfate assimilation; IEA:EnsemblFungi.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT DOMAIN 657..888
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1044 AA; 114386 MW; F587237BC774358C CRC64;
MAHQSGVKNP LEEISPVFPH SVPADISSVN GTLYTTAQTL VQQVAYTLSD KLFTYSPDTF
SLDEAARLWS GNEQTNVRGV VPTVNAMETR LGAANVLLGY VFSPDVDPKK KAVAKSIIAS
SPALIHMRSA LDQLSVLYGV SSPFVAHVSA VDYEVSSAKL VTDYASAVTV AQETGIGLLA
SFSAHEAQHM ALFATLAATV LPMVHIYDGV SVSRESAKIK DVLDRTSLQN VFSSILGEQK
EAPKKADQGT KVNAILRGLN AELGTAYSLF EYEGHDEPDA VLVTFGSVES LLATQVAASL
TNSGERIGVI AIRVYRPFSE PHFLEALPRS VKRIAVLGQV ANKAAAEDSA VQSALYVDVV
AAITMSDIWT LPPPIVDIPE EELTAQASTM DAFILLGDGS HAQQYVFWDG DDAASAPAAS
IISRLLSEDP RKSVSFQAAY DNVPLSGILH SEIRASSSAI DAPFHIECAD ISVVNDIQLL
SKFDIASRTK DSGIILLKST IKDDEFEKKL PALFRRAVTK KAINLIIADP SALGDEAPAA
VENALIQLAF AKLANISAPL EKLSYLNIDS STVHQAYERL DSSLRNVEIP KEWADSLEDN
EPSHLPTIPQ TTSFAINEEK HTTEPAPALK TSQSAAQAIV FKEAYDVQSA LRPDLSMKNY
IVKVQENRRL TPEYYGRNIF HIEFDLSGTG MEYQIGEALG IHSQNDPDEV SEFIEFYGLN
ADDIVEVPSK DDPDVLEMRT VFQALSQNVD IFGRPPKKFY ESLAEFATDE GERKALLTLS
SAEGATESKR RAEMDTVTFA DILAEYKSAH PSFYELVRIV SPLKRREYSI ASSQKVNPNS
VHLLIVVVNW VDTKGRDRFG QATRYLSRLP IGAKVTVSVK PSVMKLPPLA TQPLIMAGLG
TGLAPFRAFV QYRAWQKSQG VDIGSVLLYM GSRHQREEYL YGEEWEAYQA AGIVTLLGRA
FSRDQSEKIY IQDRMRQSLD DIIEAYIKED GAFYLCGPTW PVPDVTEVLQ EAIVEEGKRR
GAKVDGAKKI EELKEGLRYV LEVY
//
