ID S3CV77_OPHP1 Unreviewed; 322 AA.
AC S3CV77;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphoadenosine phosphosulfate reductase {ECO:0000313|EMBL:EPE04660.1};
GN ORFNames=F503_06209 {ECO:0000313|EMBL:EPE04660.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE04660.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE04660.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE04660.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate. {ECO:0000256|ARBA:ARBA00024327}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC {ECO:0000256|ARBA:ARBA00009732}.
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DR EMBL; KE148159; EPE04660.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CV77; -.
DR STRING; 1262450.S3CV77; -.
DR VEuPathDB; FungiDB:F503_06209; -.
DR eggNOG; KOG0189; Eukaryota.
DR HOGENOM; CLU_044089_0_1_1; -.
DR OMA; PIARWTQ; -.
DR OrthoDB; 1429290at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:InterPro.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00063; CysH; 1.
DR InterPro; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR011800; PAPS_reductase_CysH.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00434; cysH; 1.
DR NCBIfam; TIGR02057; PAPS_reductase; 1.
DR PANTHER; PTHR46509; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR PANTHER; PTHR46509:SF1; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR Pfam; PF01507; PAPS_reduct; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923}.
FT DOMAIN 82..270
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 35907 MW; 4C46E292CD0A746E CRC64;
MSAAISTTNS PRLDTTEVSK QADDAASVES GYGSAPPSAS SSTARLPRVT LTPEHLRHLN
KQLENMEPMD ILRFAKIFFP NLYQTTAFGL TGLVTIDILS KLGREEQAAN SSSTAPKHPV
DLIFLDTLYH FEETYDLVNR VRTQYSGINI HTFKPDGFET AAEFEATYGR LYELSEEMYD
YLAKVEPQER SYDHLEVTAV LTGRRRSQGG QRGSLDIIEV DDERGIYKIN PLANWSFGEV
QKYVREHNVP YNALLDRGYK SIGDWHSTSP VAEGEDERAG RWKGRNKTEC GIHNKQSRYA
QFLAGDATDE SATAAAPPTV TA
//
