ID A0RYU5_CENSY Unreviewed; 261 AA.
AC A0RYU5;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=CENSYa_1903 {ECO:0000313|EMBL:ABK78512.1};
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Nitrososphaerota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK78512.1, ECO:0000313|Proteomes:UP000000758};
RN [1] {ECO:0000313|EMBL:ABK78512.1, ECO:0000313|Proteomes:UP000000758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|Proteomes:UP000000758};
RX PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT symbiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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; DP000238; ABK78512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RYU5; -.
DR STRING; 414004.CENSYa_1903; -.
DR EnsemblBacteria; ABK78512; ABK78512; CENSYa_1903.
DR KEGG; csy:CENSYa_1903; -.
DR PATRIC; fig|414004.10.peg.1738; -.
DR HOGENOM; CLU_044089_1_0_2; -.
DR Proteomes; UP000000758; Chromosome.
DR GO; GO:0043866; F:adenylyl-sulfate reductase (thioredoxin) activity; IEA:RHEA.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0019344; P:cysteine biosynthetic process; 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 Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00063; CysH; 1.
DR InterPro; IPR011798; APS_reductase.
DR InterPro; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR02055; APS_reductase; 1.
DR NCBIfam; TIGR00434; cysH; 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 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 ECO:0000313|EMBL:ABK78512.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000758}.
FT DOMAIN 58..232
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 261 AA; 29278 MW; C3BB13DE7A091865 CRC64;
MKRGNPCPAP ALAIVIKENR GTGSLKFTQS EVDGLNSRID TAAGALEWAS ENLHPRVAKA
SSFGAEDAAV MDMMAGINPG FRFFTLDTGR LPEATYDAME AARKRYGIKL EVLFPDAAEV
EEMVNKSGPN LFYESVENRK LCCDIRKVRP TNKYLAGLDG WITGLRRDQT RNRGGARMFE
IDGGHGGILK INPIIEWTWE QIWAYIKEHD VPYNRLLDEG YASIGCEPCT RAIKPGEDLR
AGRWWWESNS QKECGLHVRQ K
//
