NODQ_RHIS3
ID NODQ_RHIS3 Reviewed; 646 AA.
AC P72339;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 N33).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=103798;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cloutier J.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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; U53327; AAB16902.1; -; Genomic_DNA.
DR AlphaFoldDB; P72339; -.
DR SMR; P72339; -.
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; IPR005225; Small_GTP-bd_dom.
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 TIGRFAMs; TIGR00231; small_GTP; 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..646
FT /note="Bifunctional enzyme NodQ"
FT /id="PRO_0000091543"
FT DOMAIN 25..240
FT /note="tr-type G"
FT REGION 1..461
FT /note="Sulfate adenylyltransferase"
FT REGION 34..41
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 92..96
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 113..116
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 168..171
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 205..207
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 462..646
FT /note="Adenylyl-sulfate kinase"
FT ACT_SITE 544
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 34..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 113..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 168..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 470..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 646 AA; 71489 MW; 1DBEE1DA257FE128 CRC64;
MRHIMAKSLA PTDGVRDYLA AQEKKSLLRF LTCGSVDDGK STLIGRLLSD TKQIFEDQLA
ALERDSRKHG TTGDDIDFAL LVDGLEAERE QGITIDVAYR FFATPKRKFI VADTPGHEQY
TRNMATGAST ADLAIVLIDA RQGVLRQTRR HSIIASLLGI RHIVLAVNKI DLVGFDQAVF
ERITESYRQF SRDLGFQTIV PIPMSARYGD NVTSRSESME WYSGPTLIEH LETVSVEEAV
VELPFRFPVQ YVNRPNLDFR GFAGTVASGS VAPGDEVVVA KSGKSSRVKR IVSYGGDLAQ
AAAGQAVTLV LDDEVEISRG NMLVSPAARP QVADQFAANI VWFDEHALLP GRSYILRTET
DQTSATVTDL KYRINVNDFA HEAAKSLEMN EVGICNISTR SPIAFDTFAE NRTTGAFILI
DRITNATVGA GMILHSLRRA ENIHWQSLDV GKRVRADMKH QRPAVFWFTG LSGSGKSTIA
NLFEKKLFAT GRHTYILDGD NVRHGLNRDL GFTEADRVEN IRRVAEVARL MADAGLIVIV
SFISPFSAER RMARELMADG EFVEVFVDTP FEECARRDPK GLYARALNGE IKNFTGVDSP
YEAPEKPEIH LKTLGRSAEE MVDALEHWLN ERDIAQPPPA DNGGSI
