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
