位置:首页 > 蛋白库 > CYSN_VIBCM
CYSN_VIBCM
ID   CYSN_VIBCM              Reviewed;         476 AA.
AC   C3LRM1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=VCM66_2479;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001233; ACP06776.1; -; Genomic_DNA.
DR   RefSeq; WP_001057929.1; NC_012578.1.
DR   AlphaFoldDB; C3LRM1; -.
DR   SMR; C3LRM1; -.
DR   EnsemblBacteria; ACP06776; ACP06776; VCM66_2479.
DR   GeneID; 57741161; -.
DR   KEGG; vcm:VCM66_2479; -.
DR   HOGENOM; CLU_007265_5_2_6; -.
DR   OMA; FPVQYVL; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001217; Chromosome I.
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   Transferase.
FT   CHAIN           1..476
FT                   /note="Sulfate adenylyltransferase subunit 1"
FT                   /id="PRO_1000117919"
FT   DOMAIN          24..238
FT                   /note="tr-type G"
FT   REGION          33..40
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          91..95
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          112..115
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          167..170
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          205..207
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         33..40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT   BINDING         112..116
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT   BINDING         167..170
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
SQ   SEQUENCE   476 AA;  52880 MW;  9434FBAD03A959A9 CRC64;
     MNNAVKEQLA ELGIEGYLNQ HQHKSLLRFL TCGSVDDGKS TLIGRLLHDS KQIYEDQLAA
     VHNDSQRVGT TGSRPDLALL VDGLQAEREQ GITIDVAYRY FSTQKRKFII ADTPGHEQYT
     RNMATGASTC DLAVILIDAR KGVLDQTRRH SFISNLLGLK HFIVAVNKMD LVDYSQDRFE
     QIRAEYLEFS KHLQGETEIQ IIPLSALEGD NVVEKSRLMD WYQGPSLLEL LEYVDIDRDK
     SSGAFRFPVQ YVNRPNLDFR GFAGTIASGV VKVGDKIKAL PSGKTSTVTR IVTFDGDLPQ
     AQAGLAVTLT LADEIDISRG DLIVLESAQV DSTNHLLADV VWMTEQPLQV GRDYDIKIAG
     KKTVGQVKAV RHQYDINNLS TYHAESLPLN GIGLCEWTFT QTVALDKYLD CADTGGFIII
     DRLTNVTVGA GLVRDSLQNI TGQTESFSAF ELELNALVRK HFPHWQAIDL SRLGKA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024