CYSC_PSEAE
ID CYSC_PSEAE Reviewed; 196 AA.
AC P57702; Q9I3V1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=PA1393;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate. {ECO:0000250}.
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; AE004091; AAG04782.1; -; Genomic_DNA.
DR PIR; H83472; H83472.
DR RefSeq; NP_250084.1; NC_002516.2.
DR RefSeq; WP_003112412.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; P57702; -.
DR SMR; P57702; -.
DR STRING; 287.DR97_630; -.
DR PaxDb; P57702; -.
DR EnsemblBacteria; AAG04782; AAG04782; PA1393.
DR GeneID; 877968; -.
DR KEGG; pae:PA1393; -.
DR PATRIC; fig|208964.12.peg.1442; -.
DR PseudoCAP; PA1393; -.
DR HOGENOM; CLU_046932_1_0_6; -.
DR InParanoid; P57702; -.
DR OMA; GVTIWFT; -.
DR PhylomeDB; P57702; -.
DR BioCyc; PAER208964:G1FZ6-1419-MON; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000002438; 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..196
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_0000105913"
FT ACT_SITE 105
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 22060 MW; B21D609EF21D1083 CRC64;
MNPREHGKRS IDNETRSALK RQRPAVIWLT GLSGAGKSTI ASALELALFE QKKHTFLLDG
DDLRLGLCRN LGYSDEDRTE NIRRIAEVAK ILLEAGLIVI VATISPFSRD RRLSRELIGI
EHFIEVFVDT PLSECERRDP KGLYRKARSG KIENFTGIDS IYETPAQPNI TIDTLSEDPD
LAVKRIISYL ETNQPA
