NODQ_RHIME
ID NODQ_RHIME Reviewed; 641 AA.
AC P13442;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 157.
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; OrderedLocusNames=RA0469; ORFNames=SMa0857;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RCR2011 / SU47;
RX PubMed=2546009; DOI=10.1111/j.1365-2958.1989.tb00223.x;
RA Cervantes E., Sharma S.B., Maillet F., Vasse J., Truchet G., Rosenberg C.;
RT "The Rhizobium meliloti host range nodQ gene encodes a protein which shares
RT homology with translation elongation and initiation factors.";
RL Mol. Microbiol. 3:745-755(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2520820; DOI=10.1094/mpmi-2-181;
RA Schwedock J., Long S.R.;
RT "Nucleotide sequence and protein products of two new nodulation genes of
RT Rhizobium meliloti, nodP and nodQ.";
RL Mol. Plant Microbe Interact. 2:181-194(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; X14809; CAA32914.1; -; Genomic_DNA.
DR EMBL; M68858; AAA26343.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65127.1; -; Genomic_DNA.
DR PIR; E95320; E95320.
DR PIR; S14899; ZZZRNQ.
DR RefSeq; NP_435715.1; NC_003037.1.
DR RefSeq; WP_010967450.1; NC_003037.1.
DR AlphaFoldDB; P13442; -.
DR SMR; P13442; -.
DR STRING; 266834.SM_b21224; -.
DR EnsemblBacteria; AAK65127; AAK65127; SMa0857.
DR GeneID; 61599272; -.
DR KEGG; sme:SMa0857; -.
DR PATRIC; fig|266834.11.peg.479; -.
DR eggNOG; COG0529; Bacteria.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_0_5; -.
DR OMA; TPYYDGP; -.
DR Proteomes; UP000001976; Plasmid pSymA.
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; Plasmid; Reference proteome;
KW Transferase.
FT CHAIN 1..641
FT /note="Bifunctional enzyme NodQ"
FT /id="PRO_0000091542"
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..641
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 641 AA; 70614 MW; 1E1261F04ED33A93 CRC64;
MSYVQSIPPH DIEAHLAEHD NKSILRFITC GSVDDGKSTL IGRLLYDAKL VFEDQLANLG
RVGSPGAANG KEIDLALLLD GLEAEREQGI TIDVAYRYFA TSKRKFIVAD TPGHEEYTRN
MVTGASTADL AIILIDSRQG ILQQTRRHSY IASLLGIRHV VLAVNKIDLV DFKQQVYEEI
VADYMAFAKE LGFASIRPIP ISARDGDNVI SASANTPWYR GAALLEYLET VELDPTDQAK
PFRFPVQMVM RPNADFRGYA GQISCGRISV GDPVVVAKTG QRTSVKAIVT YDGELATAGE
GEAVTLVLSD EVDASRGNML VAPGARPFVA DQFQAHVIWF DANPMMPGRS YILRTETDSV
SATVTTLKHQ VNINSFIREA AKSLQMNEVG VCNISTQAPI AFDAYNDNRA TGNFIIVDRV
TNATVGAGLI DFPLRRADNV HWHALEVNKS ARSAMKNQLP AVLWFTGLSG SGKSTIANEL
DRILHAQGKH TYLLDGDNVR HGLNRDLGFT EEDRVENIRR VAEVAKLMAD AGLIVLVSFI
SPFRDERRMA RELMEEGEFI EIFVDTPLDE CARRDPKGLY EKALAGKIAN FTGVSSCYEA
PENPELHIRT VGHQPNDLAL AIEEFLDRRI GGQMTPLQRP T
