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Database: UniProt
Entry: A4SRG8
LinkDB: A4SRG8
Original site: A4SRG8 
ID   CYSN_AERS4              Reviewed;         471 AA.
AC   A4SRG8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   29-OCT-2014, entry version 52.
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};
GN   OrderedLocusNames=ASA_3522;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A.,
RA   Kimball J., Munholland J., Murphy C., Sarty D., Williams J.,
RA   Nash J.H., Johnson S.C., Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights
RT   into the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
CC   -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_00062}.
CC   -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl
CC       sulfate. {ECO:0000255|HAMAP-Rule:MF_00062}.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00062}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and
CC       CysN. {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}.
CC   -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding)
CC       domain. {ECO:0000305}.
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DR   EMBL; CP000644; ABO91490.1; -; Genomic_DNA.
DR   RefSeq; YP_001143238.1; NC_009348.1.
DR   ProteinModelPortal; A4SRG8; -.
DR   SMR; A4SRG8; 19-433.
DR   STRING; 382245.ASA_3522; -.
DR   PRIDE; A4SRG8; -.
DR   EnsemblBacteria; ABO91490; ABO91490; ASA_3522.
DR   GeneID; 4995753; -.
DR   KEGG; asa:ASA_3522; -.
DR   PATRIC; 20793498; VBIAerSal2987_3509.
DR   eggNOG; COG2895; -.
DR   HOGENOM; HOG000229289; -.
DR   KO; K00956; -.
DR   OMA; HFVVAIN; -.
DR   OrthoDB; EOG6GR38Q; -.
DR   BioCyc; ASAL382245:GJJN-3509-MONOMER; -.
DR   UniPathway; UPA00140; UER00204.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR   InterPro; IPR000795; EF_GTP-bd_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR011779; SO4_adenylTrfase_lsu.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 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; Complete proteome; GTP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN         1    471       Sulfate adenylyltransferase subunit 1.
FT                                /FTId=PRO_1000008900.
FT   DOMAIN       24    240       tr-type G.
FT   NP_BIND      33     40       GTP. {ECO:0000255|HAMAP-Rule:MF_00062}.
FT   NP_BIND     112    116       GTP. {ECO:0000255|HAMAP-Rule:MF_00062}.
FT   NP_BIND     167    170       GTP. {ECO:0000255|HAMAP-Rule:MF_00062}.
FT   REGION       33     40       G1. {ECO:0000250}.
FT   REGION       91     95       G2. {ECO:0000250}.
FT   REGION      112    115       G3. {ECO:0000250}.
FT   REGION      167    170       G4. {ECO:0000250}.
FT   REGION      204    206       G5. {ECO:0000250}.
SQ   SEQUENCE   471 AA;  52222 MW;  DD721F84C4CF30B5 CRC64;
     MNNHIQTAIS EQGIEAYLHA QQHKSLLRFL TCGSVDDGKS TLIGRLLHDS QQIYEDQLKA
     LESDSQKLGT TGEKLDLALL VDGLQAEREQ GITIDVAYRY FSTAKRKFII SDTPGHEQYT
     RNMATGASTC DLAIILIDAR KGVLDQTRRH SFIASLLGIK QFVVAVNKMD LVEFSQEVFD
     RISADYREFA KKLNVDTIQI VPVSALDGDN VVNPSDKLAW YQGETLLSLL ESADVERELE
     RHPVRLPVQY VNRPNLDFRG FAGTLAAGIL RVGDKLAVLP SGKESTVTRI VTFDGDLEYA
     LPGQAITVTF ADEIDISRGD LLVDAAKKPQ VTQNVLAHIV WMGEESLQPG RVYDVKLATK
     KTRGQVEVIR HRIEINKLDQ LDASELHLNE IGLCEVSLTD PVAFDPYTDI RDTGSFILID
     RLTNVTVGAG MIVEGLAAKA VAGQYSEFEI ELNALVRKHF PHWQALAIGK E
//
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