ID   CYSC_VIBCH              Reviewed;         215 AA.
AC   Q9KP21;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Adenylyl-sulfate kinase;
DE            EC=2.7.1.25;
DE   AltName: Full=APS kinase;
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase;
GN   Name=cysC; OrderedLocusNames=VC_2558;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC         + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:456216; EC=2.7.1.25;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF95699.1; -; Genomic_DNA.
DR   PIR; F82062; F82062.
DR   RefSeq; NP_232186.1; NC_002505.1.
DR   RefSeq; WP_000043054.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KP21; -.
DR   SMR; Q9KP21; -.
DR   STRING; 243277.VC_2558; -.
DR   PRIDE; Q9KP21; -.
DR   DNASU; 2615575; -.
DR   EnsemblBacteria; AAF95699; AAF95699; VC_2558.
DR   GeneID; 57741160; -.
DR   KEGG; vch:VC_2558; -.
DR   PATRIC; fig|243277.26.peg.2436; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_1_0_6; -.
DR   OMA; GVTIWFT; -.
DR   BioCyc; VCHO:VC2558-MON; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02027; APSK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..215
FT                   /note="Adenylyl-sulfate kinase"
FT                   /id="PRO_0000105923"
FT   ACT_SITE        120
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  23906 MW;  83B9EE2F295CDDF6 CRC64;
     MSKQADSLGF EQDAKPENVV WHRHAVDKAQ RATLKQQRPA VLWFTGLSGA GKSTVAGALE
     NRLAALGYHT YLLDGDNVRH GLCSDLGFSE QDRRENIRRI GELAKLMSDA GLIVLTAFIS
     PHRAERQMVR DLLPNGEFLE VYVNTSLDVC EARDPKGLYK KARAGEIRQF TGIDSAYEAP
     LNPDIDLPAG EKSVDELVAQ CLQALAERHI IQRWV