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CYSN_ALIB4
ID   CYSN_ALIB4              Reviewed;         469 AA.
AC   A8EWR6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Abu_2175;
OS   Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Aliarcobacter.
OX   NCBI_TaxID=367737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM4018;
RX   PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA   Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA   Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA   Rogosin A., Stanker L.H., Mandrell R.E.;
RT   "The complete genome sequence and analysis of the Epsilonproteobacterium
RT   Arcobacter butzleri.";
RL   PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV68389.1; -; Genomic_DNA.
DR   RefSeq; WP_004511054.1; NC_009850.1.
DR   AlphaFoldDB; A8EWR6; -.
DR   SMR; A8EWR6; -.
DR   STRING; 367737.Abu_2175; -.
DR   EnsemblBacteria; ABV68389; ABV68389; Abu_2175.
DR   KEGG; abu:Abu_2175; -.
DR   eggNOG; COG2895; Bacteria.
DR   HOGENOM; CLU_007265_5_2_7; -.
DR   OMA; PGHVEYT; -.
DR   OrthoDB; 244339at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001136; 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_1000092132"
FT   DOMAIN          22..238
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          203..205
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;  53151 MW;  3BCC94E8B8D504AB CRC64;
     MSDLENKIAT DIESYLKEHE NKQLLRFITC GSVDDGKSTL IGRLLHDSKM IFEDQLAAIK
     KDSKKVGTTE GEFDLALLVD GLQSEREQGI TIDVAYRYFT TDKRKFIIAD TPGHEQYTRN
     MATGASTADL AIILIDARYG VQTQTRRHSF ITKLLGIKHI VVAVNKMDLV DFKEDIFNQI
     SSDYLKFAQE LGMTKDITLI PISALNGDNI VKRSEKSPWY KGDTLMNLLE TIKIDEDRDL
     VHFRFPVQYV NRPNLNFRGF CGTIASGVIK VGDAITVLPS GKSSTVKEIV TYDGNLDYAY
     SQQAITLTLN DEIDISRGDI IVKSDEQPDH ASNLDVDIVW MSEEPLIKGK QYFIKRATTV
     TVGSIDHFYY KTDVNTLEQS EANVLNLNEI SRAKLDLEQV IAFDSYDKNK VMGSFIIIDR
     ITNNTVGAGM IRNKSEDQSK KDSIYSDFEI EFNALVRKHF PHWECKEIF
 
 
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