CYSC_ECOLI
ID CYSC_ECOLI Reviewed; 201 AA.
AC P0A6J1; P23846; P78105; Q2MA79; Q59376; Q59389;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25 {ECO:0000269|PubMed:1332767};
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=b2750, JW2720;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-9.
RC STRAIN=K12;
RX PubMed=1316900; DOI=10.1016/s0021-9258(19)50034-5;
RA Leyh T.S., Vogt T.F., Suo Y.;
RT "The DNA sequence of the sulfate activation locus from Escherichia coli K-
RT 12.";
RL J. Biol. Chem. 267:10405-10410(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, ACTIVE SITE, AND
RP CATALYTIC ACTIVITY.
RX PubMed=1332767; DOI=10.1021/bi00162a003;
RA Satishchandran C., Hickman Y.N., Markham G.D.;
RT "Characterization of the phosphorylated enzyme intermediate formed in the
RT adenosine 5'-phosphosulfate kinase reaction.";
RL Biochemistry 31:11684-11688(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION.
RX PubMed=2828368; DOI=10.1016/s0021-9258(18)69222-1;
RA Leyh T.S., Taylor J.C., Markham G.D.;
RT "The sulfate activation locus of Escherichia coli K12: cloning, genetic,
RT and enzymatic characterization.";
RL J. Biol. Chem. 263:2409-2416(1988).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
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 Evidence={ECO:0000269|PubMed:1332767};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000305|PubMed:1332767}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR EMBL; M74586; AAA23647.1; -; Genomic_DNA.
DR EMBL; M86936; AAA23503.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69260.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75792.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76827.1; -; Genomic_DNA.
DR PIR; B65056; B65056.
DR RefSeq; NP_417230.1; NC_000913.3.
DR RefSeq; WP_001173673.1; NZ_STEB01000027.1.
DR AlphaFoldDB; P0A6J1; -.
DR SMR; P0A6J1; -.
DR BioGRID; 4263423; 19.
DR IntAct; P0A6J1; 11.
DR STRING; 511145.b2750; -.
DR PaxDb; P0A6J1; -.
DR PRIDE; P0A6J1; -.
DR EnsemblBacteria; AAC75792; AAC75792; b2750.
DR EnsemblBacteria; BAE76827; BAE76827; BAE76827.
DR GeneID; 66673376; -.
DR GeneID; 947221; -.
DR KEGG; ecj:JW2720; -.
DR KEGG; eco:b2750; -.
DR PATRIC; fig|1411691.4.peg.3990; -.
DR EchoBASE; EB0182; -.
DR eggNOG; COG0529; Bacteria.
DR HOGENOM; CLU_046932_1_0_6; -.
DR InParanoid; P0A6J1; -.
DR OMA; GVTIWFT; -.
DR PhylomeDB; P0A6J1; -.
DR BioCyc; EcoCyc:ADENYLYLSULFKIN-MON; -.
DR BioCyc; MetaCyc:ADENYLYLSULFKIN-MON; -.
DR UniPathway; UPA00140; UER00205.
DR PRO; PR:P0A6J1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IMP:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1316900"
FT CHAIN 2..201
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_0000105909"
FT ACT_SITE 109
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000269|PubMed:1332767"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 134
FT /note="T -> Q (in Ref. 1; AAA23647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22321 MW; 11E15BB8F9D2FD4B CRC64;
MALHDENVVW HSHPVTVQQR ELHHGHRGVV LWFTGLSGSG KSTVAGALEE ALHKLGVSTY
LLDGDNVRHG LCSDLGFSDA DRKENIRRVG EVANLMVEAG LVVLTAFISP HRAERQMVRE
RVGEGRFIEV FVDTPLAICE ARDPKGLYKK ARAGELRNFT GIDSVYEAPE SAEIHLNGEQ
LVTNLVQQLL DLLRQNDIIR S
