ID CYSN_SALG2 Reviewed; 479 AA.
AC B5RDQ7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 01-MAY-2013, entry version 36.
DE RecName: Full=Sulfate adenylyltransferase subunit 1;
DE EC=2.7.7.4;
DE AltName: Full=ATP-sulfurylase large subunit;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
GN Name=cysN; OrderedLocusNames=SG2837;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K.,
RA Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A.,
RA Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G.,
RA Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and
RT Salmonella gallinarum 287/91 provides insights into evolutionary and
RT host adaptation pathways.";
RL Genome Res. 18:1624-1637(2008).
CC -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl
CC sulfate.
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC from sulfate: step 1/3.
CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and
CC CysN (By similarity).
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC CysN/NodQ subfamily.
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DR EMBL; AM933173; CAR38645.1; -; Genomic_DNA.
DR RefSeq; YP_002227676.1; NC_011274.1.
DR ProteinModelPortal; B5RDQ7; -.
DR STRING; 550538.SG2837; -.
DR EnsemblBacteria; CAR38645; CAR38645; SG2837.
DR GeneID; 6923357; -.
DR KEGG; seg:SG2837; -.
DR PATRIC; 18504196; VBISalEnt1629_3001.
DR eggNOG; COG2895; -.
DR HOGENOM; HOG000229289; -.
DR KO; K00956; -.
DR OMA; HDSAQIY; -.
DR ProtClustDB; PRK05124; -.
DR BioCyc; SENT550538:GJ93-2783-MONOMER; -.
DR UniPathway; UPA00140; UER00204.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:HAMAP.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1; -.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR011779; SO4_adenylTrfase_lsu.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; Elong_init_C; 1.
DR SUPFAM; SSF50447; Translat_factor; 1.
DR TIGRFAMs; TIGR02034; CysN; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; GTP-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1 479 Sulfate adenylyltransferase subunit 1.
FT /FTId=PRO_1000092154.
FT NP_BIND 34 41 GTP (By similarity).
FT NP_BIND 113 117 GTP (By similarity).
FT NP_BIND 168 171 GTP (By similarity).
SQ SEQUENCE 479 AA; 53067 MW; 16FC19A2EEACD209 CRC64;
MNTILAQQIA NEGGVEAWMI AQQHKSLLRF LTCGSVDDGK STLIGRLLHD TLQIYEDQLS
SLHNDSKRHG TQGEKLDLAL LVDGLQAERE QGITIDVAYR YFSTEKRKFI IADTPGHEQY
TRNMATGAST CDLAILLIDA RKGVLDQTRR HSFISTLLGV KHLVVAINKM DLVDYCEETF
ARIREDYLTF AEQLPGDLDI RFVPLSALEG DNVAAQSANM RWYSGPTLLE VLETVDIQRA
VDRQPMRFPV QYVNRPNLDF RGYAGTLASG SVKVGERIKV LPSGVESSVA RIVTFDGDKE
EACAGEAITL VLNDDIDISR GDLLLAANET LAPARHAAID VVWMAEQPLA PGQSYDVKLA
GKKTRARIEA IRYQIDINNL TQRDVESLPL NGIGLVEMTF DEPLALDIYQ QNPVTGGLIF
IDRLSNVTVG AGMVRELDER GATPPVEYSA FELELNALVR RHFPHWDARD LLGDKHGAA
//
