CYSN_LARHH
ID CYSN_LARHH Reviewed; 481 AA.
AC C1D890;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=LHK_01695;
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Laribacter.
OX NCBI_TaxID=557598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9;
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO74680.1; -; Genomic_DNA.
DR RefSeq; WP_012697166.1; NC_012559.1.
DR AlphaFoldDB; C1D890; -.
DR SMR; C1D890; -.
DR STRING; 557598.LHK_01695; -.
DR PRIDE; C1D890; -.
DR EnsemblBacteria; ACO74680; ACO74680; LHK_01695.
DR KEGG; lhk:LHK_01695; -.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_2_4; -.
DR OMA; FPVQYVL; -.
DR OrthoDB; 244339at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002010; 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; 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 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..481
FT /note="Sulfate adenylyltransferase subunit 1"
FT /id="PRO_1000117915"
FT DOMAIN 22..236
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 481 AA; 53901 MW; 14AE3915869E9999 CRC64;
MTHQSDLIAE DIHAYLARHE TKDLLRFITC GSVDDGKSTL IGRLLHDSRL IFEDQLAAIE
RDSQKHNTTD EAVDLALLVD GLQAEREQGI TIDVAYRYFS TDTRKFIIAD CPGHEQYTRN
MATGASTADL AIILIDARYG VQTQTRRHSF IASLLGIRHV IVAVNKMDLL EFDQAVFERI
RQDYLTFAKA LDIHDIRFVP LSALRGDNVV SPSERMPWYD GPSLMQLLDS IRLDADQALQ
AFRLPVQYVN RPNLDFRGFC GTIAAGVIRP GDQVTVLPSG RQSRVRAIVT TDGELPVAAT
GQAVTLTLED EIDISRGDMI VRHGEPLPLV ADRLTVELVW MHDAPLQTGR AYWVKLAGKW
LPGRVTAVHH RVNVNTMERE AASSLALNEI AEVTLEIDAP MAVDAYRQCR ATGSLILVDR
ISNATLGAGM IRSAEPSAGI QSEKDAARRW QAFEIEFNEL VRRHFPHWQA RDMRDWPGHK
E
