CYSN_SALPB
ID CYSN_SALPB Reviewed; 479 AA.
AC A9N2D8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00062};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00062};
DE AltName: Full=ATP-sulfurylase large subunit {ECO:0000255|HAMAP-Rule:MF_00062};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00062};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_00062};
GN Name=cysN {ECO:0000255|HAMAP-Rule:MF_00062}; OrderedLocusNames=SPAB_03649;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- 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};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00062}.
CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC {ECO:0000255|HAMAP-Rule:MF_00062}.
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}.
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DR EMBL; CP000886; ABX68989.1; -; Genomic_DNA.
DR RefSeq; WP_001092257.1; NC_010102.1.
DR AlphaFoldDB; A9N2D8; -.
DR SMR; A9N2D8; -.
DR KEGG; spq:SPAB_03649; -.
DR PATRIC; fig|1016998.12.peg.3436; -.
DR HOGENOM; CLU_007265_5_2_6; -.
DR OMA; FPVQYVL; -.
DR BioCyc; SENT1016998:SPAB_RS14870-MON; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000008556; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..479
FT /note="Sulfate adenylyltransferase subunit 1"
FT /id="PRO_1000075067"
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 479 AA; 53124 MW; A0DD7E7BDEF26253 CRC64;
MNTILAQQIA NEGGVEAWMI AQQHKSLLRF LTCGSVDDGK STLIGRLLHD TLQIYEDQLS
SLHNDSKRHG TQGEKLDLAL LVDGLQAERE QGITIDVAYR YFSTEKRKFI IADTPGHEQY
TRNMATGAST CDLAILLIDA RKGVLDQTRR HSFISTLLGI KHLVVAINKM DLVDYREETF
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 GATPSVEYSA FELELNALVR RHFPHWDARD LLGDKHGAA
