(data stored in ACNUC7421 zone)

SWISSPROT: D1CDF4_THET1

ID   D1CDF4_THET1            Unreviewed;       248 AA.
AC   D1CDF4;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Phosphoadenosine phosphosulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE            EC=1.8.4.8 {ECO:0000256|HAMAP-Rule:MF_00063};
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   OrderedLocusNames=Tter_0037 {ECO:0000313|EMBL:ACZ40960.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40960.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40960.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Reduction of activated sulfate into sulfite.
CC       {ECO:0000256|HAMAP-Rule:MF_00063, ECO:0000256|SAAS:SAAS00769104}.
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       ECO:0000256|SAAS:SAAS00769099}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00063, ECO:0000256|SAAS:SAAS00831828}.
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DR   EMBL; CP001825; ACZ40960.1; -; Genomic_DNA.
DR   RefSeq; WP_012873995.1; NC_013525.1.
DR   STRING; 525904.Tter_0037; -.
DR   EnsemblBacteria; ACZ40960; ACZ40960; Tter_0037.
DR   KEGG; ttr:Tter_0037; -.
DR   eggNOG; ENOG4105ET3; Bacteria.
DR   eggNOG; COG0175; LUCA.
DR   HOGENOM; HOG000249397; -.
DR   KO; K00390; -.
DR   OMA; KTECGLW; -.
DR   OrthoDB; 674332at2; -.
DR   BioCyc; TTER525904:G1GGS-37-MONOMER; -.
DR   UniPathway; UPA00140; UER00206.
DR   Proteomes; UP000000323; Chromosome 1.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF000857; PAPS_reductase; 1.
DR   TIGRFAMs; TIGR00434; cysH; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDF4.
DR   SWISS-2DPAGE; D1CDF4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063,
KW   ECO:0000256|SAAS:SAAS00769124};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00063,
KW   ECO:0000256|SAAS:SAAS00831824, ECO:0000313|EMBL:ACZ40960.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   DOMAIN       45    214       PAPS_reduct. {ECO:0000259|Pfam:PF01507}.
SQ   SEQUENCE   248 AA;  28422 MW;  87755F95A230DB62 CRC64;
     MSLVDKIVEE PAKEELDRIN AELEDATPQE IIKWAVDRFG DGLILACSFG GISGMAILDM
     AVKIKPDIDV FYIDTDFLFP ETHQTKEEAI KRYGIKPIAF KTKLTPEAQA EKYGDELWKR
     NPDLCCHIRK VEPTREALKG RSAWITGLRR DQSSTRRNVR PVEWDYKFGL YKINPLAYWN
     EREVWRYIFK HNVPYNPLHD QGYPSIGCTH CTSPVYGSED SRAGRWAGTG KVECGLHIKL
     PQTESSSQ
//

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