ID Q57FJ5_BRUAB Unreviewed; 252 AA.
AC Q57FJ5;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE Short=APS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE EC=1.8.4.10 {ECO:0000256|HAMAP-Rule:MF_00063};
DE AltName: Full=5'-adenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
GN Name=cysH {ECO:0000256|HAMAP-Rule:MF_00063,
GN ECO:0000313|EMBL:AAX73589.1};
GN OrderedLocusNames=BruAb1_0178 {ECO:0000313|EMBL:AAX73589.1};
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698 {ECO:0000313|EMBL:AAX73589.1, ECO:0000313|Proteomes:UP000000540};
RN [1] {ECO:0000313|EMBL:AAX73589.1, ECO:0000313|Proteomes:UP000000540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941 {ECO:0000313|EMBL:AAX73589.1,
RC ECO:0000313|Proteomes:UP000000540};
RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
CC -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-
CC phosphosulfate (APS) using thioredoxin as an electron donor.
CC {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|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; AE017223; AAX73589.1; -; Genomic_DNA.
DR RefSeq; WP_002965431.1; NC_006932.1.
DR AlphaFoldDB; Q57FJ5; -.
DR EnsemblBacteria; AAX73589; AAX73589; BruAb1_0178.
DR GeneID; 55589970; -.
DR KEGG; bmb:BruAb1_0178; -.
DR HOGENOM; CLU_044089_2_1_5; -.
DR Proteomes; UP000000540; Chromosome I.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00063}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 46..214
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT ACT_SITE 234
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ SEQUENCE 252 AA; 27582 MW; 4F22019DE21B3144 CRC64;
MLPDADIADA DERAAAQARL LEASHGASAP HEIIALVTHE LFEGRVAVVS SFGAESAVLL
HMISQIDRAT PVLFLDTGKH FRATLDYRHQ LVGRLGLADV RDILPVADSL AKEDPFGALS
MTDKDRCCFI RKVEPMARAV APYRAWMTGR KQFQASTRNG LPVFESVGPR IRINPLARWR
AEDLRAYAEK YSLPPHPLTA QGYRSIGCMP CTRPVSEGED QRAGRWAGSE KTECGIHLSG
LADSLKGIPK AV
//
