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Database: UniProt
Entry: B2UAL6_RALPJ
LinkDB: B2UAL6_RALPJ
Original site: B2UAL6_RALPJ 
ID   B2UAL6_RALPJ            Unreviewed;       267 AA.
AC   B2UAL6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000256|ARBA:ARBA00029514, ECO:0000256|HAMAP-Rule:MF_00063};
DE            Short=APS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE            EC=1.8.4.10 {ECO:0000256|ARBA:ARBA00024386, ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=5'-adenylylsulfate reductase {ECO:0000256|ARBA:ARBA00032041, ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000256|ARBA:ARBA00030894, ECO:0000256|HAMAP-Rule:MF_00063};
GN   Name=cysH {ECO:0000256|HAMAP-Rule:MF_00063};
GN   OrderedLocusNames=Rpic_2687 {ECO:0000313|EMBL:ACD27813.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD27813.1};
RN   [1] {ECO:0000313|EMBL:ACD27813.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=12J {ECO:0000313|EMBL:ACD27813.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-
CC       phosphosulfate (APS) using thioredoxin as an electron donor.
CC       {ECO:0000256|ARBA:ARBA00024298, ECO:0000256|HAMAP-Rule:MF_00063}.
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         ECO:0000256|HAMAP-Rule:MF_00063};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00063};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00063};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate. {ECO:0000256|ARBA:ARBA00024327, ECO:0000256|HAMAP-
CC       Rule:MF_00063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000256|ARBA:ARBA00009732, ECO:0000256|HAMAP-Rule:MF_00063}.
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DR   EMBL; CP001068; ACD27813.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2UAL6; -.
DR   STRING; 402626.Rpic_2687; -.
DR   KEGG; rpi:Rpic_2687; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_044089_1_0_4; -.
DR   OMA; KTECGLW; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043866; F:adenylyl-sulfate reductase (thioredoxin) activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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   PANTHER; PTHR46482:SF9; 5'-ADENYLYLSULFATE REDUCTASE 1, CHLOROPLASTIC; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00063}.
FT   DOMAIN          59..234
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   ACT_SITE        256
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT   BINDING         145
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT   BINDING         146
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT   BINDING         228
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT   BINDING         231
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   267 AA;  29889 MW;  C11773B4A22B489C CRC64;
     MSEFQEAALS EVPVSAIGRP VLWTRPVYTG TAEALAAKEA ALFERLAEIA ARHGVAKFAT
     SLAAEDMVVT DAILRSPQAV RAHLPIFTLQ TGRLHAETLA MLERIREHYG YVIEQYAPDA
     RAVEAYVRDH GLNAFYDSIE LRKACCNIRK VVPLNRALKD ADAWLTGQRR EQAVTRADLP
     FAEDDDARGI AKYNPLFDWS EPEVWAYLEQ HNVPTNALHD KGYPSIGCEP CTRAVRAGED
     VRAGRWWWES RDSKECGLHA TNLSQKS
//
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