CYSC_BUCAP
ID CYSC_BUCAP Reviewed; 211 AA.
AC Q8K9D4;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=BUsg_407;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM67957.1; -; Genomic_DNA.
DR RefSeq; WP_011053924.1; NC_004061.1.
DR AlphaFoldDB; Q8K9D4; -.
DR SMR; Q8K9D4; -.
DR STRING; 198804.BUsg_407; -.
DR EnsemblBacteria; AAM67957; AAM67957; BUsg_407.
DR KEGG; bas:BUsg_407; -.
DR eggNOG; COG0529; Bacteria.
DR HOGENOM; CLU_046932_1_0_6; -.
DR OMA; GVTIWFT; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000000416; 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; -; 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..211
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_0000105906"
FT ACT_SITE 110
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 211 AA; 24288 MW; 0644BA855D76B6B1 CRC64;
MHNNSKKNII WQKHSVTRIK REQKNGHKSI VIWFTGLSGS GKSSIANSLE EILFQNNFNT
YLLDGDNIRS SLCSDLSFSI LDRNENIRRI GEVSKLMIDA GIIVLVSVIS PYRNQRKKIR
LMLGKINFLE VFVDTPLNIC EERDPKKLYQ KSRLGKISDL TGIQSLYEIP EKPDLHLDET
ISLKNNTKKL IHILCDKNII SFPNIDETFL F
