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CYSN_PSYIN
ID   CYSN_PSYIN              Reviewed;         469 AA.
AC   A1ST27;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Ping_0798;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000510; ABM02642.1; -; Genomic_DNA.
DR   RefSeq; WP_011769205.1; NC_008709.1.
DR   AlphaFoldDB; A1ST27; -.
DR   SMR; A1ST27; -.
DR   STRING; 357804.Ping_0798; -.
DR   EnsemblBacteria; ABM02642; ABM02642; Ping_0798.
DR   KEGG; pin:Ping_0798; -.
DR   eggNOG; COG2895; Bacteria.
DR   HOGENOM; CLU_007265_5_2_6; -.
DR   OMA; TPYYDGP; -.
DR   OrthoDB; 244339at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000000639; Chromosome.
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..469
FT                   /note="Sulfate adenylyltransferase subunit 1"
FT                   /id="PRO_1000092150"
FT   DOMAIN          22..224
FT                   /note="tr-type G"
FT   REGION          31..38
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          89..93
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          110..113
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          165..168
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          202..204
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         31..38
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT   BINDING         110..114
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT   BINDING         165..168
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
SQ   SEQUENCE   469 AA;  52610 MW;  769C300A7D920315 CRC64;
     MSNDSNLLAT DIEEYLRVHE NKDLMRFITC GSVDDGKSTL IGRLLFDSKM IFEDHMAAIE
     KDSKKFNTTD NDFDLSLLVD GLQSEREQGI TIDVAYRYFA TEQRKFIIAD TPGHEQYTRN
     MVTGASTCDL AIILIDARYG VQVQTRRHSY ICSLLGIKHL VVAVNKMDAV DYDQAVYKKI
     KADYREFAKQ LNIADIRFVP ISALKGDNVV NESENMTWYP GSPLLRLLNT IQIDTDINDK
     FRLAVQYVNR PNLDFRGFCG TVASGEIRVG DTIQALPSGK QSKVKSIVTF DGELESAFAG
     MAITLTLEDE IDISRGNMIV RPHEKPTSSK NFVADLVWMT EEALHVDREY IIKAGAHSTF
     GSVISINNKV DVNTMEKCEA NQLVLNEIGS CNFEVAEALH FDRYSENRAT GAFIMIDRLT
     NATVGAGMIS GSVEALAKTA PEYSAFEVEF NALVRKHYPH WETKDITKL
 
 
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