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CYSN_RHITR
ID   CYSN_RHITR              Reviewed;         494 AA.
AC   O33581;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   03-AUG-2022, entry version 95.
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};
OS   Rhizobium tropici.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CFN 299;
RX   PubMed=9773278; DOI=10.3109/10425179809050027;
RA   Laeremans T., Martinez-Romero E., Vanderleyden J.;
RT   "Isolation and sequencing of a second Rhizobium tropici CFN299 genetic
RT   locus that contains genes homologous to amino acid sulphate activation
RT   genes.";
RL   DNA Seq. 9:65-70(1998).
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, ECO:0000305}.
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DR   EMBL; AJ001223; CAA04619.1; -; Genomic_DNA.
DR   PIR; A58721; A58721.
DR   AlphaFoldDB; O33581; -.
DR   SMR; O33581; -.
DR   UniPathway; UPA00140; UER00204.
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   Transferase.
FT   CHAIN           1..494
FT                   /note="Sulfate adenylyltransferase subunit 1"
FT                   /id="PRO_0000091527"
FT   DOMAIN          24..240
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          204..206
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   494 AA;  53322 MW;  1D59CE43219AEAB8 CRC64;
     MTAAATANVV TLPASEPAKA VRDTRPLRLI TCGSVDDGKS TLIGRLLWDT KAVKEDQAAT
     LQRDSTGKQN DLGLPDFALL LDGLQAEREQ GITIDVAYRY FSTDKRSFIV ADTPGHEQYT
     RNMATGASTA DLAVLLVDAR MGILEQTRRH ATIASLLGIK QFVLAINKID LTNYDRAGFE
     KISHDFREFA LSLGVKQITA IPMSALKGEN VVYSGQAAMP WYTGPTLVET LELATVRSAQ
     AVGFRLSVQR VSRPGESFRG YQGTVAGGSV KPGDSVMILP SGMVANVSKI VTFDLVRNAA
     VAGDAITLVL DRQVDVSRGD MIVAIDSQPQ SGLSFDAQIV ALQPEGIEPG KRYWLKSGSR
     RQRVQVQPIA QLELKTGAWA PAQSLWMNAI GKVRLSFDEA AVFDPYDQNR STGSFILIDP
     ESNNTVAGGM ITGKRADLGG IHKDGQRVLL SLPADLADQI MASELFSSRR DETEVRRVTA
     AQAAEIWANA ASDI
 
 
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