NODQ_RHITR
ID NODQ_RHITR Reviewed; 632 AA.
AC P52978;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
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;
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=8755625; DOI=10.1094/mpmi-9-0492;
RA Laeremans T., Caluwaerts I., Verreth C., Rogel M.A., Vanderleyden J.,
RA Martinez-Romero E.;
RT "Isolation and characterization of Rhizobium tropici Nod factor sulfation
RT genes.";
RL Mol. Plant Microbe Interact. 9:492-500(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CIAT899;
RX PubMed=8850086; DOI=10.1094/mpmi-9-0151;
RA Folch-Mallol J.L., Marroqui S., Sousa C., Manyani H., Lopez-Lara I.M.,
RA van der Drift K.M.G.M., Haverkamp J., Quinto C., Gil-Serrano A.,
RA Thomas-Oates J., Spaink H.P., Megias M.;
RT "Characterization of Rhizobium tropici CIAT899 nodulation factors: the role
RT of nodH and nodPQ genes in their sulfation.";
RL Mol. Plant Microbe Interact. 9:151-163(1996).
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.
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}.
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DR EMBL; U47272; AAB08984.1; -; Genomic_DNA.
DR EMBL; X87608; CAA60914.1; -; Genomic_DNA.
DR AlphaFoldDB; P52978; -.
DR SMR; P52978; -.
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; 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; 2.
DR TIGRFAMs; TIGR00455; apsK; 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; Kinase; Multifunctional enzyme; Nodulation;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..632
FT /note="Bifunctional enzyme NodQ"
FT /id="PRO_0000091545"
FT DOMAIN 22..236
FT /note="tr-type G"
FT REGION 1..457
FT /note="Sulfate adenylyltransferase"
FT REGION 31..38
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 88..92
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 109..112
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 164..167
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 187..189
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 458..632
FT /note="Adenylyl-sulfate kinase"
FT ACT_SITE 540
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 31..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 109..113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 164..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 466..473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 632 AA; 69815 MW; 8FA3DF0CC7C604B6 CRC64;
MPYPFSISPH DMEEHLVQED KGPVLRFITC GSVDDGKSTL IGRLLCDAQL VFEDQLADLR
HGGIRGGNGE EIDFSLVLDG LEAEREQGIT IDVAYRYFST SKRKFIVADT PGHFEYTRNM
ATGASTADLA VILVDSRQGI LQQTRRHSYL ASLLGIRHVV LAVNKIDLID FSEPIFDAIV
AEYVRFSAKL GFASVMAIPM SARFGDNVVS KSGKLPWYQG SPLLEYLETV ELDAPDRQEP
FRFPVQLVMR PNADFRGYAG RIASGKIAVG DPVIVAKSGL RSSVRAIIAP DGNQISAAEG
EPVTLVLADE VDVSRGDMLV DPASRPFVSD QFQAHLIWFD ANPMLPGRSY LLRTETDSVS
ATVTVLKHQL NVDSFVREPA KLLQMNEVGV CNIMTQRPIV FDAYKENRST GNFIIVDRVS
SATVGAGMID FPLRRADNVH WQALDVDKAA RSALKNQKPA VLWLTGLSGS GKSTIANALE
ALLHTCGKHT YLLDGDNVRH GLNRDLGFTA VDRVENIRRV AEVAKLMADA GLIVICSFIS
PFRDERRMAR ELMGEGEFIE IFVDTPLDEC ARRDPKGLYK KAFAGNIANF TGVSSPYEAP
ENPELHLKTM GQEPARLALQ IEEFLRSRME EK
