ID   CYSC_SHEFN              Reviewed;         207 AA.
AC   Q07Y94;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Adenylyl-sulfate kinase;
DE            EC=2.7.1.25;
DE   AltName: Full=APS kinase;
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
GN   Name=cysC; OrderedLocusNames=Sfri_3184;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA   Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA   Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC   -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-
CC       phosphoadenylyl sulfate.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
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DR   EMBL; CP000447; ABI73020.1; -; Genomic_DNA.
DR   RefSeq; YP_751859.1; -.
DR   GeneID; 4280086; -.
DR   GenomeReviews; CP000447_GR; Sfri_3184.
DR   KEGG; sfr:Sfri_3184; -.
DR   NMPDR; fig|318167.10.peg.3057; -.
DR   HOGENOM; Q07Y94; -.
DR   OMA; Q07Y94; IVWHQHS.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR   HAMAP; MF_00065; -; 1.
DR   InterPro; IPR002891; APS_kinase_C.
DR   Pfam; PF01583; APS_kinase; 1.
DR   ProDom; PD002350; APS_kinase; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1    207       Adenylyl-sulfate kinase.
FT                                /FTId=PRO_1000009025.
FT   NP_BIND      31     38       ATP (By similarity).
FT   ACT_SITE    105    105       Phosphoserine intermediate (By
FT                                similarity).
SQ   SEQUENCE   207 AA;  22580 MW;  21E01D46448CA4EB CRC64;
     MSNIVWHQHA IDQAARGAQK GQNPVLLWFT GLSGSGKSTL AGALERALFE HGFHTYLLDG
     DNVRHGLCKD LGFSIEDRDE NLRRVGEVAK LMVDSGLVVL SAFISPTREE RDRVRALFPQ
     GQFVEVHVST PLSVCESRDP KGLYAKARKG EITNFTGISS PYEVPESAEL TIDTSKGDLD
     TQVHGLLAYL KAIDVLNPPR EIAGAGI
//