(data stored in SCRATCH3701 zone)

SWISSPROT: CYSN_VIBVY

ID   CYSN_VIBVY              Reviewed;         476 AA.
AC   Q7MPF2;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 102.
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=VV0412;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity.
CC       {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}.
DR   EMBL; BA000037; BAC93176.1; -; Genomic_DNA.
DR   RefSeq; WP_011149357.1; NC_005139.1.
DR   SMR; Q7MPF2; -.
DR   STRING; 672.VV93_v1c03820; -.
DR   PRIDE; Q7MPF2; -.
DR   EnsemblBacteria; BAC93176; BAC93176; BAC93176.
DR   GeneID; 2623179; -.
DR   KEGG; vvy:VV0412; -.
DR   PATRIC; fig|196600.6.peg.444; -.
DR   HOGENOM; HOG000229289; -.
DR   KO; K00956; -.
DR   OMA; SRGDMIC; -.
DR   OrthoDB; 244339at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000002675; Chromosome I.
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   HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR   InterPro; IPR041757; CysN_GTP-bd.
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; TF_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;
DR   PRODOM; Q7MPF2.
DR   SWISS-2DPAGE; Q7MPF2.
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_0000091535"
FT   DOMAIN          24..243
FT                   /note="tr-type G"
FT   NP_BIND         33..40
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT   NP_BIND         112..116
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT   NP_BIND         167..170
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
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"
SQ   SEQUENCE   476 AA;  52658 MW;  A6999E9B40E279D2 CRC64;
     MNSAVQAQLA ELGIEGYLNQ HQHKSLLRFL TCGSVDDGKS TLIGRLLHDS KQIYEDQLAA
     VHSDSQRVGT TGSRPDLALL VDGLQAEREQ GITIDVAYRY FSTQKRKFII ADTPGHEQYT
     RNMATGASTC DLAVILIDAR KGVLDQTRRH SFISNLLGLK HFVVAVNKMD LVEFSQQRFE
     EIKAEYLAFS KNLRGETDIQ IIPISALEGD NVVELSQQMA WYQGPTLLEI LEAVDVEKEK
     EAGEFRFPVQ YVNRPNLDFR GFAGTISSGV VKVGDRITAL PSGKSSTVAR IVTFDGDLEQ
     AQAGLAVTLT LADEIDISRG DLIVHHGANV ELTNHLAADV VWMTEQPLQP GRDYDIKIAG
     KKTIGRVEHI HHQYDINNLS KHSAAELPLN GIGLCEWTFN ESIALDNYQD CADTGGFIII
     DRLTNVTVGA GMVSESLTEV TKASSDFSAF ELELNALIRK HFPHWDAKDL SELLKK
//

If you have problems or comments...

PBIL Back to PBIL home page