(data stored in ACNUC7421 zone)

SWISSPROT: Q3KJ29_PSEPF

ID   Q3KJ29_PSEPF            Unreviewed;       203 AA.
AC   Q3KJ29;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 102.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774032};
DE            EC=2.7.1.25 {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774032};
DE   AltName: Full=APS kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00065};
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
GN   Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065,
GN   ECO:0000313|EMBL:ABA72227.1};
GN   OrderedLocusNames=Pfl01_0483 {ECO:0000313|EMBL:ABA72227.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72227.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72227.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72227.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347,
CC       ECO:0000256|SAAS:SAAS00774005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl
CC         sulfate + 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:0000256|HAMAP-
CC         Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065,
CC       ECO:0000256|RuleBase:RU004347}.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00065, ECO:0000256|RuleBase:RU004347,
CC       ECO:0000256|SAAS:SAAS01092250}.
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DR   EMBL; CP000094; ABA72227.1; -; Genomic_DNA.
DR   RefSeq; WP_011332148.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0483; -.
DR   EnsemblBacteria; ABA72227; ABA72227; Pfl01_0483.
DR   KEGG; pfo:Pfl01_0483; -.
DR   eggNOG; ENOG4108EKF; Bacteria.
DR   eggNOG; COG0529; LUCA.
DR   HOGENOM; HOG000228204; -.
DR   KO; K00860; -.
DR   OMA; IVWHQHS; -.
DR   BioCyc; PFLU205922:G1G4S-488-MONOMER; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000002704; 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:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02027; APSK; 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;
DR   PRODOM; Q3KJ29.
DR   SWISS-2DPAGE; Q3KJ29.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS01092249,
KW   ECO:0000313|EMBL:ABA72227.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347, ECO:0000313|EMBL:ABA72227.1}.
FT   NP_BIND      41     48       ATP. {ECO:0000256|HAMAP-Rule:MF_00065}.
FT   ACT_SITE    115    115       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00065}.
SQ   SEQUENCE   203 AA;  22414 MW;  EEF8209C271184B0 CRC64;
     MNEALHSLAT TPAISPYNLA LPRQARAALN GQRPRCLWLT GLSGAGKSTL ANSLELHLHQ
     FGRHTFLLDG DNVRNGLCRD LGMDDAGRRE NIRRMAEVAR LMVDAGLIVI VAAISPFRAE
     RDAARRLFAE GDFVEVHVST SLTVCERRDP KGLYQAVRQG RIQHFTGIDS PYEAPLAAEC
     RIDTEEIEPS EACERLAALL LEK
//

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