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 01-MAY-2013, entry version 43.
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=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 (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; 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; HDSAQIY; -.
DR ProtClustDB; PRK05124; -.
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: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 1 471 Sulfate adenylyltransferase subunit 1.
FT /FTId=PRO_1000008900.
FT NP_BIND 33 40 GTP (By similarity).
FT NP_BIND 112 116 GTP (By similarity).
FT NP_BIND 167 170 GTP (By similarity).
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
//
