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NODQ_AZOBR
ID   NODQ_AZOBR              Reviewed;         620 AA.
AC   P28604; Q6QW77;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Bifunctional enzyme NodQ;
DE   AltName: Full=Nodulation protein Q;
DE   Includes:
DE     RecName: Full=Sulfate adenylyltransferase subunit 1;
DE              EC=2.7.7.4;
DE     AltName: Full=ATP-sulfurylase large subunit;
DE     AltName: Full=Sulfate adenylate transferase;
DE              Short=SAT;
DE   Includes:
DE     RecName: Full=Adenylyl-sulfate kinase;
DE              EC=2.7.1.25;
DE     AltName: Full=APS kinase;
DE     AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
GN   Name=nodQ; ORFNames=pRhico026;
OS   Azospirillum brasilense.
OG   Plasmid pRhico (90-MDa megaplasmid).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=2131098; DOI=10.1094/mpmi-3-389;
RA   Vieille C., Elmerich C.;
RT   "Characterization of two Azospirillum brasilense Sp7 plasmid genes
RT   homologous to Rhizobium meliloti nodPQ.";
RL   Mol. Plant Microbe Interact. 3:389-400(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=15033235; DOI=10.1016/s0378-1097(04)00046-1;
RA   Vanbleu E., Marchal K., Lambrecht M., Mathys J., Vanderleyden J.;
RT   "Annotation of the pRhico plasmid of Azospirillum brasilense reveals its
RT   role in determining the outer surface composition.";
RL   FEMS Microbiol. Lett. 232:165-172(2004).
CC   -!- FUNCTION: Proposed to provide activated sulfate for transfer to Nod
CC       factor. ATP sulfurylase may be the GTPase, regulating ATP sulfurylase
CC       activity (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: APS kinase catalyzes the synthesis of activated sulfate.
CC       {ECO:0000250}.
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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC         + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:456216; EC=2.7.1.25;
CC   -!- SUBUNIT: Sulfate-activating enzymes, NodP and NodQ, may be physically
CC       associated. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class
CC       translation factor GTPase superfamily. Classic translation factor
CC       GTPase family. CysN/NodQ subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is not obvious if the APS kinase domain is functional; the
CC       conserved active site serine (position 527) is replaced by an alanine.
CC       {ECO:0000305}.
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DR   EMBL; M94886; AAA22186.1; -; Genomic_DNA.
DR   EMBL; AY523973; AAS83003.1; -; Genomic_DNA.
DR   PIR; I39755; I39755.
DR   RefSeq; WP_035683262.1; NZ_VITX01000018.1.
DR   AlphaFoldDB; P28604; -.
DR   SMR; P28604; -.
DR   GeneID; 56449450; -.
DR   OrthoDB; 244339at2; -.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02027; APSK; 1.
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; -; 2.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR041757; CysN_GTP-bd.
DR   InterPro; IPR044138; CysN_II.
DR   InterPro; IPR044139; CysN_NoDQ_III.
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; 2.
DR   TIGRFAMs; TIGR00455; apsK; 1.
DR   TIGRFAMs; TIGR02034; CysN; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GTP-binding; Kinase; Multifunctional enzyme; Nodulation;
KW   Nucleotide-binding; Nucleotidyltransferase; Plasmid; Transferase.
FT   CHAIN           1..620
FT                   /note="Bifunctional enzyme NodQ"
FT                   /id="PRO_0000091541"
FT   DOMAIN          7..223
FT                   /note="tr-type G"
FT   REGION          1..444
FT                   /note="Sulfate adenylyltransferase"
FT   REGION          16..23
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          74..78
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          95..98
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          150..153
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          187..189
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   REGION          445..620
FT                   /note="Adenylyl-sulfate kinase"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         95..99
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         453..460
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        113
FT                   /note="A -> R (in Ref. 1; AAA22186)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   620 AA;  66956 MW;  5DABE4AF9E763BC9 CRC64;
     METGTGRGLL RFLTCGSVDD GKSTLIGRLL HDAGLISDDQ LEQARRDSRG RAEEDGGIDF
     SLLVDGLEAE REQSITIDVA YRYFATDRRS FIVADAPGHE QYTRNMATAA SGASLAVLLV
     DARKGLLTQT RRHAIVASLM GIRHVVLAVN KMDLVEDGET VFAAIRQAFT VFSAPLGFRS
     VTAIPLSARH GDNVVHRSAA MPWHHGPTLL GHLETAAAED DPTEDGPLRF LVEWVNRPNL
     DFRGLSGTLL SGSLETGGAV TVWPSGRSAR IARIVTFDGD VTQARAGDAV TVTLDAAVDA
     GRGDLLSGPD GAPEVADQFA AHLLWMAEEP LIPGRSYLLR AGARWVPATV TALRHAVNVE
     TLEHGAASVL GLNAVGLCNL STAAPLAFDP YEASRHTGSF ILVDRFSNRT VGAGMIRHPL
     RRAANLHRQE LAVSTVERAA LKRQRPAVLW FTGLSGSGKS TIANRVERRL HTLGHHTMML
     DGDNVRLGLN RDLGFTDADR VENIRRVGEV AKLMTEAGLI VLCAFIAPFR AEREAVRALL
     PDGAFLEVFV DTPLDECMRR DPKGLYAKAR AGTLRNFTGV DSPYEAPDAP ELRLDTTAED
     ADALAERVVE LLHRKGIAEA
 
 
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