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CYSN_SHEWM
ID   CYSN_SHEWM              Reviewed;         469 AA.
AC   B1KMH4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Swoo_1687;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) 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; CP000961; ACA85972.1; -; Genomic_DNA.
DR   RefSeq; WP_012324318.1; NC_010506.1.
DR   AlphaFoldDB; B1KMH4; -.
DR   SMR; B1KMH4; -.
DR   STRING; 392500.Swoo_1687; -.
DR   PRIDE; B1KMH4; -.
DR   EnsemblBacteria; ACA85972; ACA85972; Swoo_1687.
DR   KEGG; swd:Swoo_1687; -.
DR   eggNOG; COG2895; Bacteria.
DR   HOGENOM; CLU_007265_5_2_6; -.
DR   OMA; TPYYDGP; -.
DR   OrthoDB; 244339at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000002168; 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_1000092159"
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   469 AA;  52737 MW;  F7E98DFC08B8A00E CRC64;
     MTTSSNLISS DIEEYLKVHE NKDMLRVLTC GSVDDGKSTL IGRLLFDSKM IFEDQMAAIE
     KDSKRFNTTD DSFDLALLVD GLQSEREQGI TIDVAYRYFT TEQRKFIIAD TPGHEQYTRN
     MATGASTCDL AIILIDARHG VQVQTRRHSF ICSQLGIKHV IIAINKMDAI DYDQATYQKI
     KKEYREFAED LSFSDVRFVP ISALKGDNVV NESPNMTWYP GSTLLKLLNT VSVEQDRSES
     FRFQVQYVNR PNLDFRGFCG TIGSGEIRVG DTVATLPSNK ESRVKSIVTF DGELEKAVAG
     QAVTLTLEDE IDISRGDMLV RPHDKPFSVS HFEADVVWMT EEPLCVDREY AIKVGSKSVY
     GYADAINHKV DVNTLEKQSA QQLALNEIGN CHFAVTEPVQ FDAYDTNRST GSFIIIDRLT
     NVTVGAGMIR NPIEVKSTKA HEYSEFEIEM NALVRKHFPH WGAKDISKG
 
 
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