CYSC_SHEON
ID CYSC_SHEON Reviewed; 205 AA.
AC Q8EB13;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000255|HAMAP-Rule:MF_00065};
DE EC=2.7.1.25 {ECO:0000255|HAMAP-Rule:MF_00065};
DE AltName: Full=APS kinase {ECO:0000255|HAMAP-Rule:MF_00065};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00065};
DE AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000255|HAMAP-Rule:MF_00065};
GN Name=cysC {ECO:0000255|HAMAP-Rule:MF_00065}; OrderedLocusNames=SO_3723;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000255|HAMAP-Rule:MF_00065}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00065};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_00065}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00065}.
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DR EMBL; AE014299; AAN56707.1; -; Genomic_DNA.
DR RefSeq; NP_719263.1; NC_004347.2.
DR RefSeq; WP_011073511.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EB13; -.
DR SMR; Q8EB13; -.
DR STRING; 211586.SO_3723; -.
DR PaxDb; Q8EB13; -.
DR KEGG; son:SO_3723; -.
DR PATRIC; fig|211586.12.peg.3605; -.
DR eggNOG; COG0529; Bacteria.
DR HOGENOM; CLU_046932_1_0_6; -.
DR OMA; GVTIWFT; -.
DR OrthoDB; 1574819at2; -.
DR PhylomeDB; Q8EB13; -.
DR BioCyc; SONE211586:G1GMP-3461-MON; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000008186; Chromosome.
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..205
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_0000105918"
FT ACT_SITE 105
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
SQ SEQUENCE 205 AA; 22298 MW; 09177973129AB6F4 CRC64;
MSNIVWHQHS VDQAARARLK GQNPVLLWFT GLSGAGKSTL AGALERALFE AGFHTYLLDG
DNVRHGLCKD LGFSVADRDE NLRRVGEVAK LMVDAGLVVL SAFISPTREE RDSIRARFPE
GQFIEVHVST PLSVCELRDP KGLYVKARKG EIAHFTGISS PYEAPLSAEL TIDTSKGDLA
SQVHALIDYL TAIDVISSNR LASLA