ID   A0A1M7P524_9PSED        Unreviewed;       632 AA.
AC   A0A1M7P524;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   22-NOV-2017, entry version 7.
DE   RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00062};
DE            EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00062};
DE   AltName: Full=ATP-sulfurylase large subunit {ECO:0000256|HAMAP-Rule:MF_00062};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00062};
DE            Short=SAT {ECO:0000256|HAMAP-Rule:MF_00062};
GN   Name=cysN {ECO:0000256|HAMAP-Rule:MF_00062};
GN   ORFNames=SAMN05216593_10896 {ECO:0000313|EMBL:SHN11664.1};
OS   Pseudomonas asturiensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1190415 {ECO:0000313|EMBL:SHN11664.1, ECO:0000313|Proteomes:UP000183983};
RN   [1] {ECO:0000313|EMBL:SHN11664.1, ECO:0000313|Proteomes:UP000183983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26898 {ECO:0000313|EMBL:SHN11664.1,
RC   ECO:0000313|Proteomes:UP000183983};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00062}.
CC   -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl
CC       sulfate. {ECO:0000256|HAMAP-Rule:MF_00062,
CC       ECO:0000256|SAAS:SAAS00366877}.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00062}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and
CC       CysN. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00062}.
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DR   EMBL; FRDA01000008; SHN11664.1; -; Genomic_DNA.
DR   RefSeq; WP_073168329.1; NZ_FRDA01000008.1.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000183983; Unassembled WGS sequence.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:InterPro.
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; cd02027; APSK; 1.
DR   HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR   InterPro; IPR002891; APS_kinase.
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; 2.
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 {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00444459};
KW   Complete proteome {ECO:0000313|Proteomes:UP000183983};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00055993}; Kinase {ECO:0000313|EMBL:SHN11664.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00055970};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00056011, ECO:0000313|EMBL:SHN11664.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00056018, ECO:0000313|EMBL:SHN11664.1}.
FT   DOMAIN       22    241       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      31     38       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     110    114       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     165    168       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
SQ   SEQUENCE   632 AA;  69029 MW;  BE0B773EAF1CB665 CRC64;
     MSHQSDLISE DILAYLGQHE RKEMLRFLTC GNVDDGKSTL IGRLLHDSKM IYEDHLEAIT
     RDSKKSGTTG DDVDLALLVD GLQAEREQGI TIDVAYRYFS TAKRKFIIAD TPGHEQYTRN
     MATGASTCDL AIILVDARYG VQTQTRRHSY IASLLGIKHI VVAINKMDLN GFDESVFESI
     KADYLKFADG IAFKPTTMAF VPMSALKGDN VVNRSERSPW YTGQSLMEIL ETVEIASDRN
     YTDLRFPVQY VNRPNLNFRG FAGTLASGIV HKGDEIVVLP SGKSSRVKSI VTFEGELEQA
     GPGQAVTLTM EDEIDISRGD LLVHADNVPQ VSDAFDAMLV WMAEEPMLPG KKYDIKRATS
     YVPGSIASIT HRVDVNTLVE GPASSLQLNE IGRVKISLDA PIALDGYDSN RTTGAFIVID
     RLTNGTVAAG MIIAKPVNAG GATHHGDLAH VTTQERAQRF GQQPATVLFS GLSGAGKSTL
     AYAVERKLFD MGRAVYVLDG QNLRHDLNKG LPQNRAGRTE NWSRAAHVAR QFNEAGLLTL
     AAFVAPDAEG RERVKALIGK ERLVTVYVQA SPAVCRERDP QGLYAADGDN IPGESFPYDV
     PLDADLVIDT QALTVDEGVK LVLDMLRSRG AI
//