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Database: UniProt
Entry: M2W7R1_GALSU
LinkDB: M2W7R1_GALSU
Original site: M2W7R1_GALSU 
ID   M2W7R1_GALSU            Unreviewed;       422 AA.
AC   M2W7R1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000256|ARBA:ARBA00029514};
DE            EC=1.8.4.10 {ECO:0000256|ARBA:ARBA00024386};
DE   AltName: Full=5'-adenylylsulfate reductase {ECO:0000256|ARBA:ARBA00032041};
DE   AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000256|ARBA:ARBA00030894};
GN   ORFNames=Gasu_09200 {ECO:0000313|EMBL:EME31846.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME31846.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
CC   -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-
CC       phosphosulfate (APS) using thioredoxin as an electron donor.
CC       {ECO:0000256|ARBA:ARBA00024298}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + AMP + 2 H(+) + sulfite =
CC         [thioredoxin]-dithiol + adenosine 5'-phosphosulfate;
CC         Xref=Rhea:RHEA:21976, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:58243, ChEBI:CHEBI:456215;
CC         EC=1.8.4.10; Evidence={ECO:0000256|ARBA:ARBA00024280};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate. {ECO:0000256|ARBA:ARBA00024327}.
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DR   EMBL; KB454489; EME31846.1; -; Genomic_DNA.
DR   RefSeq; XP_005708366.1; XM_005708309.1.
DR   AlphaFoldDB; M2W7R1; -.
DR   STRING; 130081.M2W7R1; -.
DR   EnsemblPlants; EME31846; EME31846; Gasu_09200.
DR   GeneID; 17090464; -.
DR   Gramene; EME31846; EME31846; Gasu_09200.
DR   KEGG; gsl:Gasu_09200; -.
DR   eggNOG; KOG0189; Eukaryota.
DR   eggNOG; KOG1752; Eukaryota.
DR   OMA; PLKAQGY; -.
DR   OrthoDB; 457540at2759; -.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0033741; F:adenylyl-sulfate reductase (glutathione) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043866; F:adenylyl-sulfate reductase (thioredoxin) activity; IEA:RHEA.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:InterPro.
DR   CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR011798; APS_reductase.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02055; APS_reductase; 1.
DR   PANTHER; PTHR46482:SF9; 5'-ADENYLYLSULFATE REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR46482; 5'-ADENYLYLSULFATE REDUCTASE 3, CHLOROPLASTIC; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EME31846.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680}.
FT   DOMAIN          106..284
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   DOMAIN          335..397
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   422 AA;  48022 MW;  94B8A89217B81C10 CRC64;
     MFMKPLAYIN TTSTLSSSLF YSQKKAAVEK SSKTGFIAQP SRQLVCRPKD GRKWSKQEII
     YQNRKHETLD CVASADLDIP LLEKQFSVAD PQEVVNFALS TFGEEVAIAF SGAEDVVLLE
     YAKRSGKPFR VFALDTGRLH PETYRFYEKV SEYFKISIEY QFPNAEEVEA LVREKGLFSF
     YKDGHGECCG IRKVKPLKKK LSSLRAWMTG QRKDQSPSTR SFVPTIQIDP SFQGKDGTSL
     VKLNPLANRS SEQVWSMIRA LELPYNELHE RGFISIGCEP CTRPVLPNQH EREGRWWWEE
     AIQKECGLHK GNLSSTGMEE VASQLVENLI EKEPIVIFAR SDCPFCKQAK ALLDALSIAY
     KLVEMDKVEN GAELFEVLKK KTGQKTVPNI FISQKHIGGW TQLEQLYRRD LLKVNISSLQ
     IS
//
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