GenomeNet

Database: UniProt
Entry: K0IIF5_NITGG
LinkDB: K0IIF5_NITGG
Original site: K0IIF5_NITGG 
ID   K0IIF5_NITGG            Unreviewed;       179 AA.
AC   K0IIF5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
DE            EC=2.7.1.25 {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
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   OrderedLocusNames=Ngar_c08900 {ECO:0000313|EMBL:AFU57832.1};
OS   Nitrososphaera gargensis (strain Ga9.2).
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC   Nitrososphaeraceae; Nitrososphaera.
OX   NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU57832.1, ECO:0000313|Proteomes:UP000008037};
RN   [1] {ECO:0000313|EMBL:AFU57832.1, ECO:0000313|Proteomes:UP000008037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX   PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA   Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA   Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA   Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA   Spieck E., Streit W., Wagner M.;
RT   "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT   insights into metabolic versatility and environmental adaptations.";
RL   Environ. Microbiol. 14:3122-45(2012).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347}.
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:0000256|HAMAP-
CC         Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002408; AFU57832.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0IIF5; -.
DR   STRING; 1237085.Ngar_c08900; -.
DR   KEGG; nga:Ngar_c08900; -.
DR   PATRIC; fig|1237085.11.peg.848; -.
DR   HOGENOM; CLU_046932_2_1_2; -.
DR   InParanoid; K0IIF5; -.
DR   OrthoDB; 28808at2157; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000008037; 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: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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008037};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00065}.
FT   ACT_SITE        85
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   179 AA;  20094 MW;  8E671E414C2ED566 CRC64;
     MRKGFVLWLT GLPGSGKTTI SGILKQQLQS RGLQVEILDG DEVRKNLSPN LGFSKEDREI
     HAKRVAYVSQ LLARNGINVI VALISPYRSF RDNARAMIGE GFFEVWVKAS PETCRQRDPK
     GLYKKASAGQ ISNLTGIQDT YEEPLNPELV VDTEARNVNE CVNMILGLLK QYRYLSNHD
//
DBGET integrated database retrieval system