ID   CYSC_ECOL5              Reviewed;         201 AA.
AC   Q0TEA8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=ECP_2732;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000247; ABG70721.1; -; Genomic_DNA.
DR   RefSeq; YP_670622.1; -.
DR   GeneID; 4191557; -.
DR   GenomeReviews; CP000247_GR; ECP_2732.
DR   KEGG; ecp:ECP_2732; -.
DR   HOGENOM; Q0TEA8; -.
DR   OMA; Q0TEA8; IITITAF.
DR   BioCyc; ECOL362663:ECP_2732-MON; -.
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    201       Adenylyl-sulfate kinase.
FT                                /FTId=PRO_1000009011.
FT   NP_BIND      35     42       ATP (By similarity).
FT   ACT_SITE    109    109       Phosphoserine intermediate (By
FT                                similarity).
SQ   SEQUENCE   201 AA;  22320 MW;  5ABD192EE36679BB CRC64;
     MALHDENVVW HSHPVTPQQR EQHHGHRGVV LWFTGLSGSG KSTVAGGLEE ALHKLGVSTY
     LLDGDNVRHG LCSDLGFSDA DRKENIRRVG EVANLMVEAG LVVLTAFISP HRAERQMVRE
     RVGEGRFIEV FVDTPLAICE ARDPKGLYKK ARAGELRNFT GIDSVYEAPE SAEIHLNGEQ
     LVTNLVQQLL DLLRQNDIIR S
//