ID G3B6J4_CANTC Unreviewed; 253 AA.
AC G3B6J4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Phosphoadenosine phosphosulphate reductase domain-containing protein {ECO:0000259|Pfam:PF01507};
GN ORFNames=CANTEDRAFT_106520 {ECO:0000313|EMBL:EGV63486.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV63486.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996524; EGV63486.1; -; Genomic_DNA.
DR RefSeq; XP_006687279.1; XM_006687216.1.
DR AlphaFoldDB; G3B6J4; -.
DR STRING; 590646.G3B6J4; -.
DR GeneID; 18245894; -.
DR KEGG; cten:CANTEDRAFT_106520; -.
DR eggNOG; KOG0189; Eukaryota.
DR HOGENOM; CLU_044089_0_1_1; -.
DR OrthoDB; 1429290at2759; -.
DR Proteomes; UP000000707; 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 PIRSF; PIRSF000857; PAPS_reductase; 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:UP000000707}.
FT DOMAIN 37..209
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 253 AA; 29049 MW; 1824D4A7A2604047 CRC64;
MSIHITPEQL THINQQLAQL TPQEIIRWSY ITFPQLYQIT AFGLTGLVTI DMISKMNLEV
DLVFIDTLFH FPQTLELVDK VEQKYGKSVT VFKPNGFDTE KQFTDVHGSL WETDDLKYDF
LVKVEPLQRA YKQLNINAVL TGRRGSQGGD RSNLPFVEID HEFNIIKINP FLTWKFDQVQ
QYVTENSVPY NELLNLGYKS VGDWHSTEPV ADGEDERSGR WKGKAKTECG IHSTSKYALY
LKNQALGEQQ KAA
//
