CYSN_ECOLI
ID CYSN_ECOLI Reviewed; 475 AA.
AC P23845; Q2MA78;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Sulfate adenylyltransferase subunit 1;
DE EC=2.7.7.4 {ECO:0000269|PubMed:2828368, ECO:0000269|PubMed:8003495};
DE AltName: Full=ATP-sulfurylase large subunit;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
GN Name=cysN; OrderedLocusNames=b2751, JW2721;
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 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 [5]
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 [6]
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 CysD 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_00062,
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_00062, 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: GTPase activity is coupled to stimulation of the
CC rate of APS formation. {ECO:0000269|PubMed:8003495}.
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00062,
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_00062}.
CC -!- INTERACTION:
CC P23845; P21156: cysD; NbExp=2; IntAct=EBI-559728, EBI-1130200;
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. CysN/NodQ
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00062, ECO:0000305}.
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DR EMBL; M74586; AAA23646.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69261.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75793.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76828.1; -; Genomic_DNA.
DR PIR; JN0327; JN0327.
DR RefSeq; NP_417231.1; NC_000913.3.
DR RefSeq; WP_001090361.1; NZ_SSZK01000017.1.
DR AlphaFoldDB; P23845; -.
DR SMR; P23845; -.
DR BioGRID; 4262932; 28.
DR BioGRID; 851551; 1.
DR ComplexPortal; CPX-4471; Sulfate adenylyltransferase complex.
DR DIP; DIP-513N; -.
DR IntAct; P23845; 3.
DR STRING; 511145.b2751; -.
DR jPOST; P23845; -.
DR PaxDb; P23845; -.
DR PRIDE; P23845; -.
DR EnsemblBacteria; AAC75793; AAC75793; b2751.
DR EnsemblBacteria; BAE76828; BAE76828; BAE76828.
DR GeneID; 947219; -.
DR KEGG; ecj:JW2721; -.
DR KEGG; eco:b2751; -.
DR PATRIC; fig|1411691.4.peg.3989; -.
DR EchoBASE; EB0191; -.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_2_6; -.
DR InParanoid; P23845; -.
DR OMA; FPVQYVL; -.
DR PhylomeDB; P23845; -.
DR BioCyc; EcoCyc:CYSN-MON; -.
DR BioCyc; MetaCyc:CYSN-MON; -.
DR SABIO-RK; P23845; -.
DR UniPathway; UPA00140; UER00204.
DR PRO; PR:P23845; -.
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:0005525; F:GTP binding; ISS:EcoliWiki.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoliWiki.
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: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; IMP:EcoliWiki.
DR CDD; cd04166; CysN_ATPS; 1.
DR CDD; cd03695; CysN_NodQ_II; 1.
DR CDD; cd04095; CysN_NoDQ_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR InterPro; IPR041757; CysN_GTP-bd.
DR InterPro; IPR044138; CysN_II.
DR InterPro; IPR044139; CysN_NoDQ_III.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR011779; SO4_adenylTrfase_lsu.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02034; CysN; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; GTP-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..475
FT /note="Sulfate adenylyltransferase subunit 1"
FT /id="PRO_0000091522"
FT DOMAIN 25..239
FT /note="tr-type G"
FT REGION 34..41
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 92..96
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 113..116
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 168..171
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 206..208
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 34..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT BINDING 113..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT BINDING 168..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
SQ SEQUENCE 475 AA; 52558 MW; 91E983E49732AA15 CRC64;
MNTALAQQIA NEGGVEAWMI AQQHKSLLRF LTCGSVDDGK STLIGRLLHD TRQIYEDQLS
SLHNDSKRHG TQGEKLDLAL LVDGLQAERE QGITIDVAYR YFSTEKRKFI IADTPGHEQY
TRNMATGAST CELAILLIDA RKGVLDQTRR HSFISTLLGI KHLVVAINKM DLVDYSEETF
TRIREDYLTF AGQLPGNLDI RFVPLSALEG DNVASQSESM PWYSGPTLLE VLETVEIQRV
VDAQPMRFPV QYVNRPNLDF RGYAGTLASG RVEVGQRVKV LPSGVESNVA RIVTFDGDRE
EAFAGEAITL VLTDEIDISR GDLLLAADEA LPAVQSASVD VVWMAEQPLS PGQSYDIKIA
GKKTRARVDG IRYQVDINNL TQREVENLPL NGIGLVDLTF DEPLVLDRYQ QNPVTGGLIF
IDRLSNVTVG AGMVHEPVSQ ATAAPSEFSA FELELNALVR RHFPHWGARD LLGDK
