ID Q8S2V8_CHLRE Unreviewed; 413 AA.
AC Q8S2V8;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=5'-adenylylsulfate reductase {ECO:0000313|EMBL:AAM18118.1};
DE EC=1.8.4.9 {ECO:0000313|EMBL:AAM18118.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000313|EMBL:AAM18118.1};
RN [1] {ECO:0000313|EMBL:AAM18118.1}
RP NUCLEOTIDE SEQUENCE.
RA Gonzalez-Ravina C., Chang C.-I., Tsakraklides G.P., McDermott J.P.,
RA Vega J.M., Leustek T., Gotor C., Davies J.P.;
RT "Transcriptional and Post-transcriptional Control of Cysteine Biosynthesis
RT in Chlamydomonas reinhardtii.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AF498290; AAM18118.1; -; mRNA.
DR AlphaFoldDB; Q8S2V8; -.
DR ProMEX; Q8S2V8; -.
DR ExpressionAtlas; Q8S2V8; baseline and differential.
DR GO; GO:0033741; F:adenylyl-sulfate reductase (glutathione) activity; IEA:UniProtKB-EC.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:InterPro.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:InterPro.
DR CDD; cd01713; PAPS_reductase; 1.
DR CDD; cd02993; PDI_a_APS_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; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004508; Thioredoxin-indep_APS_Rdtase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR00424; APS_reduc; 1.
DR PANTHER; PTHR46482:SF9; 5'-ADENYLYLSULFATE REDUCTASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR46482; 5'-ADENYLYLSULFATE REDUCTASE 3, CHLOROPLASTIC; 1.
DR Pfam; PF01507; PAPS_reduct; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAM18118.1}.
FT DOMAIN 291..412
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 413 AA; 46426 MW; 620A13D5A9F2E402 CRC64;
MMLTQGRAFA AQRPAVQQRR MAVRANVARV PQVNAAAVEA KPDWAGLAAE MDNKSPLEIM
DHALKTFGND VAIAFSGAED VALIEYAHLT GRPYRVFSLD TGRLNPETYQ LFDAVEKHYK
IRIEYTFPEA QEVMDLVRAK GLYSFYEDGH TECCRIRKVK PLRKQLKVYK AWITGQRKDQ
SPGTRTEVPV VQVDPVFEGV TGGPGSLIKY NPLSNMTSAE VWNFLRVMKV PTNKLHNCGY
ISIGCEPCTR PVLPNQAERE GRWWWEDAAA KECGLHSGNI KKADGTTEER KAERDLWPAG
SAVATLSKDE VRALAAGERS QGTLAVLYAP WCPFCQAMEA NFEELAKHMT GHKVRVAKYQ
ADIDREFCNE NLQLKTFPTI VYLPPNSKQV IKYPSERRDV DTLSMWVKTV AGQ
//
