ID   CYSH_PSEAE              Reviewed;         267 AA.
AC   O05927;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Phosphoadenosine phosphosulfate reductase;
DE            EC=1.8.4.8;
DE   AltName: Full=PAPS reductase, thioredoxin dependent;
DE   AltName: Full=PAdoPS reductase;
DE   AltName: Full=3'-phosphoadenylylsulfate reductase;
DE   AltName: Full=PAPS sulfotransferase;
GN   Name=cysH; OrderedLocusNames=PA1756;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CHA;
RX   MEDLINE=97361814; PubMed=9218775;
RX   DOI=10.1046/j.1365-2958.1997.4121799.x;
RA   Delic-Attree I., Toussaint B., Garin J., Vignais P.M.;
RT   "Cloning, sequence and mutagenesis of the structural gene of
RT   Pseudomonas aeruginosa CysB, which can activate algD transcription.";
RL   Mol. Microbiol. 24:1275-1284(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Reduction of activated sulfate into sulfite.
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + sulfite +
CC       thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
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DR   EMBL; U95379; AAB53743.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG05145.1; -; Genomic_DNA.
DR   PIR; H83426; H83426.
DR   RefSeq; NP_250447.1; -.
DR   PDB; 2GOY; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-267.
DR   PDBsum; 2GOY; -.
DR   GeneID; 878560; -.
DR   GenomeReviews; AE004091_GR; PA1756.
DR   KEGG; pae:PA1756; -.
DR   NMPDR; fig|208964.1.peg.1757; -.
DR   PseudoCAP; PA1756; -.
DR   HOGENOM; O05927; -.
DR   OMA; O05927; TRFNGLK.
DR   BioCyc; PAER208964:PA1756-MON; -.
DR   BRENDA; 1.8.4.10; 354.
DR   BRENDA; 1.8.4.8; 354.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredo...; IEA:HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfa...; IEA:HAMAP.
DR   HAMAP; MF_00063; -; 1.
DR   InterPro; IPR011798; APS_reductase.
DR   InterPro; IPR004511; PAdo_PSO4_Rdtase_CysH.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   TIGRFAMs; TIGR02055; APS_reductase; 1.
DR   TIGRFAMs; TIGR00434; cysH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Oxidoreductase.
FT   CHAIN         1    267       Phosphoadenosine phosphosulfate
FT                                reductase.
FT                                /FTId=PRO_0000100638.
FT   CONFLICT      2      2       L -> P (in Ref. 1; AAB53743).
FT   HELIX        30     37
FT   HELIX        42     53
FT   STRAND       57     60
FT   HELIX        67     76
FT   STRAND       82     85
FT   HELIX        92    105
FT   STRAND      110    112
FT   HELIX       116    126
FT   HELIX       130    134
FT   HELIX       137    143
FT   HELIX       145    153
FT   STRAND      156    159
FT   HELIX       164    166
FT   STRAND      176    179
FT   TURN        181    183
FT   STRAND      186    188
FT   STRAND      191    193
FT   TURN        195    198
FT   HELIX       201    210
FT   HELIX       217    221
FT   HELIX       229    231
FT   HELIX       241    244
SQ   SEQUENCE   267 AA;  30215 MW;  E9557E1970F21049 CRC64;
     MLPFATIPAT ERNSAAQHQD PSPMSQPFDL PALASSLADK SPQDILKAAF EHFGDELWIS
     FSGAEDVVLV DMAWKLNRNV KVFSLDTGRL HPETYRFIDQ VREHYGIAID VLSPDPRLLE
     PLVKEKGLFS FYRDGHGECC GIRKIEPLKR KLAGVRAWAT GQRRDQSPGT RSQVAVLEID
     GAFSTPEKPL YKFNPLSSMT SEEVWGYIRM LELPYNSLHE RGYISIGCEP CTRPVLPNQH
     EREGRWWWEE ATHKECGLHA GNLISKA
//