ID A0A074ME33_9BACL Unreviewed; 228 AA.
AC A0A074ME33;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=EL26_06355 {ECO:0000313|EMBL:KEO84082.1};
OS Tumebacillus flagellatus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Tumebacillus.
OX NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO84082.1, ECO:0000313|Proteomes:UP000027931};
RN [1] {ECO:0000313|EMBL:KEO84082.1, ECO:0000313|Proteomes:UP000027931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GST4 {ECO:0000313|EMBL:KEO84082.1,
RC ECO:0000313|Proteomes:UP000027931};
RX PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT bacterium isolated from cassava wastewater.";
RL Int. J. Syst. Evol. Microbiol. 63:3138-3142(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, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEO84082.1}.
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DR EMBL; JMIR01000006; KEO84082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074ME33; -.
DR STRING; 1157490.EL26_06355; -.
DR eggNOG; COG0175; Bacteria.
DR Proteomes; UP000027931; Unassembled WGS sequence.
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 NCBIfam; TIGR00434; cysH; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000027931}.
FT DOMAIN 34..204
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 209..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ SEQUENCE 228 AA; 25896 MW; 06362707D858CBCE CRC64;
MLLTAEQVAE LNEQYVGKTP QEILQLAFEK FDNISFACSF GAEDVALVDM IVKIKPDAKI
FYLDTDVLFE ETYQVRDEIL NKYSANLIKY SPLLTLEEQA DQHGDNLWSN DPNACCNIRK
VEPLTRALST LDAWITGIRR DQAPTRANAG VIEVDTKFNL IKFNPIALWT WEDVWAYIRA
NDVPYNKLHD QNYPSIGCIH CTRAVAPGED PRAGRWSGND KTECGLHK
//