ID   NODM_RHILV              Reviewed;         608 AA.
AC   P08633;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE            Short=GFAT;
DE            EC=2.6.1.16;
DE   AltName: Full=Nodulation protein M;
GN   Name=nodM;
OS   Rhizobium leguminosarum bv. viciae.
OG   Plasmid sym pRL1JI.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=248;
RX   PubMed=3132583; DOI=10.1111/j.1365-2958.1988.tb00019.x;
RA   Surin B.P., Downie J.A.;
RT   "Characterization of the Rhizobium leguminosarum genes nodLMN involved in
RT   efficient host-specific nodulation.";
RL   Mol. Microbiol. 2:173-183(1988).
CC   -!- FUNCTION: Involved in the production of the root hair deformation (HAD)
CC       factor specifically on medicago.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; Y00548; CAA68626.1; -; Genomic_DNA.
DR   PIR; S01040; S01040.
DR   AlphaFoldDB; P08633; -.
DR   SMR; P08633; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Glutamine amidotransferase; Nodulation;
KW   Plasmid; Repeat; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..608
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135436"
FT   DOMAIN          2..217
FT                   /note="Glutamine amidotransferase type-2"
FT   DOMAIN          283..422
FT                   /note="SIS 1"
FT   DOMAIN          456..598
FT                   /note="SIS 2"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        603
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   608 AA;  65794 MW;  8D2DEF05E0A70E70 CRC64;
     MCGIVGIVGH KPVSERLIEA LGRLEYRGYD SSGVATIFEG ELHRRRAEGK LGNLKTRLKE
     APLSGTVGIA HTRWATHGAP TECNAHPHFT DGVAVVHNGI IENFSKLKDA LAEVGTKFQT
     DTDTEVIAHL LTKFRRDGMG CLEAMHAMLK CVEGAFALAI LFEDDPATIM VARNGPPLVI
     GHGDGEMFLG SDAIALAPFT NDITYLNDGD WAVVGKTSVQ VFDIEGNVVT RPRHISLATA
     DLVGKGNHPH FMEKEIYEQP EVIARALGHY INVNDSHVTT TSTDIDFAGV ESLAISACGT
     AYLAGLIGKY WFERYARLIV EIDVASEFRY REIPLSPRSA ALFISQSGET ADTLASLRYC
     KAHGLRIGAV VNTRESTMAR EADAIFPILA GPEIGVASTK AFTCQLAVLA ALRIGAGKAR
     GTITDDEEQV LVQSLATLPG VMRQVLNDIT PEIELLSREL SHYRDVLYLG RGTSFPLAME
     GALKLKEVSY IHAEGYAAGE LKHGPIALID ENMPVIVIAP HDRFFDKTVS NMQEVAARGG
     RIILITDETG ASMSKLPTMH TIVLPDVAEI IAPMIFSLPL QLLAYHTAVV MGADVDQPRN
     LAKSVTVE