CYSN_VIBPA
ID CYSN_VIBPA Reviewed; 476 AA.
AC Q87SX9;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=VP0293;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC58556.1; -; Genomic_DNA.
DR RefSeq; NP_796672.1; NC_004603.1.
DR RefSeq; WP_005454657.1; NC_004603.1.
DR AlphaFoldDB; Q87SX9; -.
DR SMR; Q87SX9; -.
DR STRING; 223926.28805275; -.
DR EnsemblBacteria; BAC58556; BAC58556; BAC58556.
DR GeneID; 1187760; -.
DR KEGG; vpa:VP0293; -.
DR PATRIC; fig|223926.6.peg.284; -.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_2_6; -.
DR OMA; FPVQYVL; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002493; Chromosome 1.
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 Reference proteome; Transferase.
FT CHAIN 1..476
FT /note="Sulfate adenylyltransferase subunit 1"
FT /id="PRO_0000091533"
FT DOMAIN 24..239
FT /note="tr-type G"
FT REGION 33..40
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 91..95
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 112..115
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 167..170
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 205..207
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT BINDING 112..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT BINDING 167..170
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
SQ SEQUENCE 476 AA; 52594 MW; 5432F92207A24B74 CRC64;
MNSAVEAQLA ELGIEGYLKQ HQYKSLLRFL TCGSVDDGKS TLIGRLLHDS KQIYEDQLAA
VHSDSQRVGT TGEKPDLALL VDGLQAEREQ GITIDVAYRY FSTQKRKFII ADTPGHEQYT
RNMATGASTC DLAVILVDAR KGILDQTRRH SFISNLLGLK HFVVAINKMD LVDYSQARFE
EIRDEYLKFS ENLTGDIDIQ IIPISALEGD NVVDKGQNLN WFEGPSLLEL LETVDVDYEK
GAGEFRFPVQ YVNRPNLDFR GFAGTVSSGS VKVGDAIKAL PSGKTSTVAR IVTFDGDIEE
AQAGLAVTLT LNDEIDISRG DLIVLENAQV QTTNHLLADV VWMTEQPLQP GRDYDIKIAG
KKTVGHVESI RHQYDINNLS THGAAELPLN GIGLCEWSLN ESVALDNYQD CADTGGFIII
DRLTNVTVGA GMVKESLTEL ERGLADVSAF ELELNALVRK HFPHWEAKDL SQLLKK
