ID   NODQ_AZOBR     STANDARD;      PRT;   620 AA.
AC   P28604; Q6QW77;
DT   01-DEC-1992 (Rel. 24, Created)
DT   25-OCT-2004 (Rel. 45, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   NodQ bifunctional enzyme (Nodulation protein Q) [Includes: Sulfate
DE   adenylyltransferase subunit 1 (EC 2.7.7.4) (Sulfate adenylate
DE   transferase) (SAT) (ATP-sulfurylase large subunit); Adenylyl-sulfate
DE   kinase (EC 2.7.1.25) (APS kinase) (ATP adenosine-5'-phosphosulfate 3'-
DE   phosphotransferase)].
GN   Name=nodQ; ORFNames=pRhico026;
OS   Azospirillum brasilense.
OG   Plasmid pRhico (90-MDa megaplasmid).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sp7 / ATCC 29145;
RX   MEDLINE=92033082; PubMed=2131098;
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.
RC   STRAIN=Sp7 / ATCC 29145;
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
RT   its 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
CC       Nod factor. ATP sulfurylase may be the GTPase, regulating ATP
CC       sulfurylase activity (By similarity).
CC   -!- FUNCTION: APS kinase catalyzes the synthesis of activated sulfate
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl
CC       sulfate.
CC   -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-
CC       phosphoadenylyl sulfate.
CC   -!- SUBUNIT: Sulfate-activating enzymes, nodP and nodQ, may be
CC       physically associated (Potential).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the GTP-binding
CC       elongation factor family. CysN/nodQ subfamily.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC       family.
CC   -!- CAUTION: It is not obvious if the APS kinase domain is functional;
CC       the conserved active site serine (position 527) is replaced by an
CC       alanine.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M94886; AAA22186.1; -.
DR   EMBL; AY523973; AAS83003.1; -.
DR   PIR; I39755; I39755.
DR   HSSP; P32324; 1N0U.
DR   HAMAP; MF_00062; fused; 1.
DR   HAMAP; MF_00065; fused; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR004161; EFTU_D2.
DR   InterPro; IPR009001; Elong_init_C.
DR   InterPro; IPR000795; ProtSyn_GTPbind.
DR   InterPro; IPR009000; Translat_factor.
DR   Pfam; PF01583; APS_kinase; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   ProDom; PD002350; APS_kinase; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; FALSE_NEG.
KW   ATP-binding; GTP-binding; Kinase; Multifunctional enzyme; Nodulation;
KW   Nucleotidyltransferase; Plasmid; Transferase.
FT   DOMAIN        1    444       Sulfate adenylyltransferase.
FT   DOMAIN      445    620       Adenylyl-sulfate kinase.
FT   NP_BIND      16     23       GTP (By similarity).
FT   NP_BIND      95     99       GTP (By similarity).
FT   NP_BIND     150    153       GTP (By similarity).
FT   NP_BIND     453    460       ATP (Potential).
FT   CONFLICT    113    113       A -> R (in Ref. 1).
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
//