CYSD_ECOLI
ID CYSD_ECOLI Reviewed; 302 AA.
AC P21156; Q2MA77;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Sulfate adenylyltransferase subunit 2;
DE EC=2.7.7.4 {ECO:0000269|PubMed:2828368, ECO:0000269|PubMed:8003495};
DE AltName: Full=ATP-sulfurylase small subunit;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
GN Name=cysD; OrderedLocusNames=b2752, JW2722;
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 1-5.
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 [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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC STRAIN=K12;
RX PubMed=2185135; DOI=10.1016/0378-1119(90)90504-k;
RA Malo M.S., Loughlin R.E.;
RT "Promoter elements and regulation of expression of the cysD gene of
RT Escherichia coli K-12.";
RL Gene 87:127-131(1990).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RX PubMed=8003495; DOI=10.1021/bi00189a036;
RA Liu C., Suo Y., Leyh T.S.;
RT "The energetic linkage of GTP hydrolysis and the synthesis of activated
RT sulfate.";
RL Biochemistry 33:7309-7314(1994).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the
CC adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and
CC diphosphate, the first enzymatic step in sulfur assimilation pathway.
CC APS synthesis involves the formation of a high-energy phosphoric-
CC sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled
CC to ATP hydrolysis by CysD. {ECO:0000255|HAMAP-Rule:MF_00064,
CC ECO:0000269|PubMed:2828368, ECO:0000269|PubMed:8003495}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00064, ECO:0000269|PubMed:2828368,
CC ECO:0000269|PubMed:8003495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18134;
CC Evidence={ECO:0000269|PubMed:2828368, ECO:0000269|PubMed:8003495};
CC -!- ACTIVITY REGULATION: Stimulated by an intrinsic GTPase (Probably CysN).
CC {ECO:0000269|PubMed:8003495}.
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00064,
CC ECO:0000269|PubMed:2828368, ECO:0000269|PubMed:8003495}.
CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC {ECO:0000255|HAMAP-Rule:MF_00064}.
CC -!- INTERACTION:
CC P21156; P23845: cysN; NbExp=2; IntAct=EBI-1130200, EBI-559728;
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00064, ECO:0000305}.
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DR EMBL; M74586; AAA23645.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69262.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75794.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76829.1; -; Genomic_DNA.
DR EMBL; M35098; AAA74892.1; -; Genomic_DNA.
DR PIR; D65056; D65056.
DR RefSeq; NP_417232.1; NC_000913.3.
DR RefSeq; WP_000372108.1; NZ_STEB01000027.1.
DR AlphaFoldDB; P21156; -.
DR SMR; P21156; -.
DR BioGRID; 4263040; 26.
DR BioGRID; 851549; 1.
DR ComplexPortal; CPX-4471; Sulfate adenylyltransferase complex.
DR DIP; DIP-360N; -.
DR IntAct; P21156; 5.
DR STRING; 511145.b2752; -.
DR jPOST; P21156; -.
DR PaxDb; P21156; -.
DR PRIDE; P21156; -.
DR EnsemblBacteria; AAC75794; AAC75794; b2752.
DR EnsemblBacteria; BAE76829; BAE76829; BAE76829.
DR GeneID; 66673374; -.
DR GeneID; 947217; -.
DR KEGG; ecj:JW2722; -.
DR KEGG; eco:b2752; -.
DR PATRIC; fig|1411691.4.peg.3988; -.
DR EchoBASE; EB0183; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_043026_0_0_6; -.
DR InParanoid; P21156; -.
DR OMA; LMIDTGH; -.
DR PhylomeDB; P21156; -.
DR BioCyc; EcoCyc:CYSD-MON; -.
DR BioCyc; MetaCyc:CYSD-MON; -.
DR SABIO-RK; P21156; -.
DR UniPathway; UPA00140; UER00204.
DR PRO; PR:P21156; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009336; C:sulfate adenylyltransferase complex (ATP); IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IDA:EcoCyc.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR GO; GO:0019419; P:sulfate reduction; IDA:ComplexPortal.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:EcoCyc.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00064; Sulf_adenylyltr_sub2; 1.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011784; SO4_adenylTrfase_ssu.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF002936; CysDAde_trans; 1.
DR TIGRFAMs; TIGR02039; CysD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="Sulfate adenylyltransferase subunit 2"
FT /id="PRO_0000100664"
FT CONFLICT 180
FT /note="S -> T (in Ref. 1; AAA23645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 35188 MW; A48881C0E5E086A1 CRC64;
MDQIRLTHLR QLEAESIHII REVAAEFSNP VMLYSIGKDS SVMLHLARKA FYPGTLPFPL
LHVDTGWKFR EMYEFRDRTA KAYGCELLVH KNPEGVAMGI NPFVHGSAKH TDIMKTEGLK
QALNKYGFDA AFGGARRDEE KSRAKERIYS FRDRFHRWDP KNQRPELWHN YNGQINKGES
IRVFPLSNWT EQDIWQYIWL ENIDIVPLYL AAERPVLERD GMLMMIDDNR IDLQPGEVIK
KRMVRFRTLG CWPLTGAVES NAQTLPEIIE EMLVSTTSER QGRVIDRDQA GSMELKKRQG
YF
