(data stored in SCRATCH zone)

SWISSPROT: Q3IFM0_PSEHT

ID   Q3IFM0_PSEHT            Unreviewed;       246 AA.
AC   Q3IFM0;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Phosphoadenosine phosphosulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063, ECO:0000256|SAAS:SAAS00751299};
DE            EC=1.8.4.8 {ECO:0000256|HAMAP-Rule:MF_00063, ECO:0000256|SAAS:SAAS00769130};
DE   AltName: Full=3'-phosphoadenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAPS reductase, thioredoxin dependent {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAPS sulfotransferase {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAdoPS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
GN   Name=cysH {ECO:0000256|HAMAP-Rule:MF_00063,
GN   ECO:0000313|EMBL:CAI85260.1};
GN   OrderedLocusNames=PSHAa0156 {ECO:0000313|EMBL:CAI85260.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85260.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85260.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Reduction of activated sulfate into sulfite.
CC       {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate +
CC         2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-
CC         dithiol; Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343; EC=1.8.4.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00063, ECO:0000256|SAAS:SAAS01124644};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 3/3. {ECO:0000256|HAMAP-Rule:MF_00063,
CC       ECO:0000256|SAAS:SAAS00831826}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00063, ECO:0000256|SAAS:SAAS00831828}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CR954246; CAI85260.1; -; Genomic_DNA.
DR   RefSeq; WP_011326875.1; NC_007481.1.
DR   STRING; 326442.PSHAa0156; -.
DR   EnsemblBacteria; CAI85260; CAI85260; PSHAa0156.
DR   KEGG; pha:PSHAa0156; -.
DR   PATRIC; fig|326442.8.peg.150; -.
DR   eggNOG; ENOG4105ET3; Bacteria.
DR   eggNOG; COG0175; LUCA.
DR   HOGENOM; HOG000249396; -.
DR   KO; K00390; -.
DR   OMA; VGDWHSS; -.
DR   OrthoDB; 674332at2; -.
DR   BioCyc; PHAL326442:PSHA_RS00795-MONOMER; -.
DR   UniPathway; UPA00140; UER00206.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
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; -; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR011800; PAPS_reductase_CysH.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF000857; PAPS_reductase; 1.
DR   TIGRFAMs; TIGR00434; cysH; 1.
DR   TIGRFAMs; TIGR02057; PAPS_reductase; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IFM0.
DR   SWISS-2DPAGE; Q3IFM0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00063,
KW   ECO:0000256|SAAS:SAAS00831824, ECO:0000313|EMBL:CAI85260.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN       47    217       PAPS_reduct. {ECO:0000259|Pfam:PF01507}.
SQ   SEQUENCE   246 AA;  28244 MW;  DBD633DD07A28C19 CRC64;
     MSEFKNILQL DKQSQTSMLA DANGILKNMS AEQRVQWALE NLPETHFLSS SFGIQAAVML
     HLITLQQPDI PVVLTDTGYL FPQTYQFIEQ MTARLSLNLK VYKSELSPAW QEAKFGKLWE
     QGEAGIKQYN QLNKVEPMTR ALKEINAGTW FSGLRRDQAS SRADKQVIEI SRGTVKVYPI
     IEWTNRDVYQ YLTKHNLPYH PLWEEGYVSM GDIHTTRKLE PGMTEEETRF FGLNRECGLH
     IDGDGI
//

If you have problems or comments...

PBIL Back to PBIL home page