NODQ_RHISB
ID NODQ_RHISB Reviewed; 633 AA.
AC O07309;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 sp. (strain BR816).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Ensifer; unclassified Ensifer.
OX NCBI_TaxID=1057002;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9421916; DOI=10.1099/00221287-143-12-3933;
RA Laeremans T., Coolsaet N., Verreth C., Snoeck C., Hellings N.,
RA Vanderleyden J., Martinez-Romero E.;
RT "Functional redundancy of genes for sulphate activation enzymes in
RT Rhizobium sp. BR816.";
RL Microbiology 143:3933-3942(1997).
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}.
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DR EMBL; U59507; AAB95249.1; -; Genomic_DNA.
DR AlphaFoldDB; O07309; -.
DR SMR; O07309; -.
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..633
FT /note="Bifunctional enzyme NodQ"
FT /id="PRO_0000091544"
FT DOMAIN 22..236
FT /note="tr-type G"
FT REGION 1..458
FT /note="Sulfate adenylyltransferase"
FT REGION 31..38
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 89..93
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 110..113
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 165..168
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 202..204
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 459..633
FT /note="Adenylyl-sulfate kinase"
FT ACT_SITE 541
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 110..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 165..168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 633 AA; 69280 MW; 696BCA683D4B3111 CRC64;
MSYLQSVPPH DLAAHLADHD GKSVLRFITC GSVDDGKSTL IGRLLVDAKL VFEDQLTNLG
RVGSSGAVNG GEIDLALLLD GLEAEREQGI TIDVAYRYFA TSKRKFIVAD TPGHEEYTRN
MVTGASTADL AVILIDSRQG ILQQTRRHSY IASLLGIRHV VLAVNKIDLV EFRQSVFDEI
ARDYKAFAKK LGFASIQPIP IAARFGDNVI SASPNTPWYK GPALLEYLET VQLDPPATER
PFRFPVQLVM RPNANFRGYA GQIASGSVSV GDPVVIAKSG QRSSVKAIVT FDGNLTTAAE
GEAVTLVLAD EVDASRGNML VAPAARPFVA DQFQAHVIWF DANPMLPGRS YILRTETDSV
SATVTALKHQ VNINSFAREA AKSLQMNEVG VCNISTQAPI VFDAYKESRA TGNFVFVDRV
TNATVGAGMI DFPLRRADNV HWQATDVNKG ARSAMKSQRP AVLWFTGLSG SGKSTIANAL
DRLLHARGKH TYMLDGDNVR HGLNRDLGFT EADRVENIRR VAEVAKLMAD AGLIVLVSFI
SPFRGERRMA RELMEEGEFI EIFVDTPLEE CARRDPKALY EKALAGKIAN FTGVSSPYEA
PESPELHLKT VEEDPVALAL KIEAFLDRHR EEK
