CYSC_PARPJ
ID CYSC_PARPJ Reviewed; 179 AA.
AC B2T3K5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Bphyt_1758;
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD16166.1; -; Genomic_DNA.
DR RefSeq; WP_012432775.1; NC_010681.1.
DR AlphaFoldDB; B2T3K5; -.
DR SMR; B2T3K5; -.
DR STRING; 398527.Bphyt_1758; -.
DR EnsemblBacteria; ACD16166; ACD16166; Bphyt_1758.
DR KEGG; bpy:Bphyt_1758; -.
DR eggNOG; COG0529; Bacteria.
DR HOGENOM; CLU_046932_1_0_4; -.
DR OMA; DIVWHEA; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000001739; Chromosome 1.
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; -; 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; Transferase.
FT CHAIN 1..179
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_1000202409"
FT ACT_SITE 87
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
SQ SEQUENCE 179 AA; 19265 MW; 1C691F1B0ECDC3C6 CRC64;
MSASRGAVIW MTGLSGAGKS TLANALHQRL MEAGHAAIVL DGDVLRRGLN ADLGFTPEDR
TENLRRIAHV AALFMQQGFV VIAAVISPEH RHRCSAREIV GDGFIEVFVN APLNVCEARD
AKGLYARARR GEIPHFTGIS GPFEAPLAPD VVIESDRMPV DESVDRLLAH LAAMGRPGH
