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CYSC_RHOBA
ID   CYSC_RHOBA              Reviewed;         247 AA.
AC   Q7UQW3;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   03-AUG-2022, entry version 100.
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=RB6049;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294143; CAD74583.1; -; Genomic_DNA.
DR   RefSeq; NP_867039.1; NC_005027.1.
DR   AlphaFoldDB; Q7UQW3; -.
DR   SMR; Q7UQW3; -.
DR   STRING; 243090.RB6049; -.
DR   EnsemblBacteria; CAD74583; CAD74583; RB6049.
DR   KEGG; rba:RB6049; -.
DR   PATRIC; fig|243090.15.peg.2917; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_1_1_0; -.
DR   InParanoid; Q7UQW3; -.
DR   OrthoDB; 1574819at2; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IBA:GO_Central.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IBA:GO_Central.
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..247
FT                   /note="Adenylyl-sulfate kinase"
FT                   /id="PRO_0000105915"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
FT   BINDING         55..62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   247 AA;  26990 MW;  0EEA0EDF8D6A4315 CRC64;
     MSQSNSDDSA SSSTQQAGDG QDDVQQNIVW HAHTVSREDR ESKLGQRGVV VWFTGLSGCG
     KSTIANELDR LLIDRGATCT LLDGDNVRHG LCAPPSVLKE EHGEDFAGRF GLGFGPTDRE
     ENIRRIGAVT ELFASAGVIV LAAFVSPYQR DRDRVRNTIE SSGRAGDFLE VFVDTPLEIC
     KQRDPKGLYQ KAIAGEIKNF TGISDPYDAP PSPEIHLKWR EGQTPHDQAS EIIREMEKRG
     VLGPAKG
 
 
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