位置:首页 > 蛋白库 > CYSN_CITK8
CYSN_CITK8
ID   CYSN_CITK8              Reviewed;         475 AA.
AC   A8ANW5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=CKO_04112;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-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}.
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; CP000822; ABV15178.1; -; Genomic_DNA.
DR   RefSeq; WP_012134867.1; NC_009792.1.
DR   AlphaFoldDB; A8ANW5; -.
DR   SMR; A8ANW5; -.
DR   STRING; 290338.CKO_04112; -.
DR   EnsemblBacteria; ABV15178; ABV15178; CKO_04112.
DR   GeneID; 45137749; -.
DR   KEGG; cko:CKO_04112; -.
DR   HOGENOM; CLU_007265_5_2_6; -.
DR   OMA; FPVQYVL; -.
DR   OrthoDB; 244339at2; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000008148; 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..475
FT                   /note="Sulfate adenylyltransferase subunit 1"
FT                   /id="PRO_1000008901"
FT   DOMAIN          25..239
FT                   /note="tr-type G"
FT   REGION          34..41
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          92..96
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          113..116
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          168..171
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          206..208
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..41
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT   BINDING         113..117
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT   BINDING         168..171
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
SQ   SEQUENCE   475 AA;  52326 MW;  85A396C085FAFDE5 CRC64;
     MNTTLAQQIA NEGGVEAWMV AQQHKSLLRF LTCGSVDDGK STLIGRLLHD TRQIYEDQLS
     SLHNDSKRHG TQGEKLDLAL LVDGLQAERE QGITIDVAYR YFSTEKRKFI IADTPGHEQY
     TRNMATGAST CDLAILLIDA RKGVLDQTRR HSFISTLLGI KHLVVAINKM DLVGFSEETF
     ARIREDYLTF AGQLPGNRDI RFVPLSALEG DNVATQSASM PWYNGPTLLE VLETVEIQRV
     VDTQPMRFPV QYVNRPNLDF RGYAGTLASG SVKVGQRIKV LPSGVESNVA RIVTFDGDLQ
     EAHAGEAITL VLKDEIDISR GDLLLDAGEN LPAVQSAAVD VVWMAEQPLS AGQSYDIKIA
     GKKTRARVDA IRHQVDINNL TQREVESLPL NGIGLVELTF DEPLVLDTYQ QNPVTGGLII
     IDRLSNVTVG AGLVREPIEH TAATPSGFSD FELELNALIR RHFPHWGARD LLGGK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024