ID   NODM_RHIML              Reviewed;         605 AA.
AC   P25195;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 99.
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 meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AK631;
RX   PubMed=1909418; DOI=10.1007/bf00282455;
RA   Baev N., Endre G., Petrovics G., Banfalvi Z., Kondorosi A.;
RT   "Six nodulation genes of nod box locus 4 in Rhizobium meliloti are involved
RT   in nodulation signal production: nodM codes for D-glucosamine synthetase.";
RL   Mol. Gen. Genet. 228:113-124(1991).
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}.
CC   -!- INDUCTION: In response to a plant signal such as luteolin via the
CC       regulatory gene NodD.
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DR   EMBL; X58632; CAA41485.1; -; Genomic_DNA.
DR   PIR; S16561; S16561.
DR   AlphaFoldDB; P25195; -.
DR   SMR; P25195; -.
DR   STRING; 382.DU99_09045; -.
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   2: Evidence at transcript level;
KW   Aminotransferase; Cytoplasm; Glutamine amidotransferase; Nodulation;
KW   Plasmid; Repeat; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..605
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135438"
FT   DOMAIN          2..216
FT                   /note="Glutamine amidotransferase type-2"
FT   DOMAIN          280..420
FT                   /note="SIS 1"
FT   DOMAIN          454..595
FT                   /note="SIS 2"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        600
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   605 AA;  65606 MW;  CA21C431400AC731 CRC64;
     MCGIVGIVGH QPVSERLVEA LEPLEYRGYD SAGVATMDAG TLQRRRAEGK LGNLREKLKE
     APLSGTIGIA HTRWATHGAP TERNAHPHFT EGVAVVHNGI IENFAELKDE LAAGGAEFQT
     ETDTEVVAHL LAKYRRDGLG RREAMHAMLK RVKGAYALAV LFEDDPSTIM AARTGPLAIG
     HGNGEMFLGS DAIALAPFTN EITYLIDGDW AVIGKTGVHI FDFDGNVVER PRQISTAAAF
     LVDKGNHRHF MEKEIYEQPE VIAIALGHYV NVIDKSCRSD SDAIDFAGVE SLAISCCGTA
     YLAGLIGKYW FERYARLPVE IAVASEFRYR EIPLSPQSAL FISQSGETAD TLASLRYCKA
     HGLRIGAVVN ARESTMARES DAVFPILAGP EIGVARTKAF TCQLAVLAAL RAGAGKARGT
     ISGDEEQALI KSLAEMPAIM GQVLNSIQPE IEVLSRELSN CRDVLYLGRG TSFPLAMEGA
     LKLKEISYIQ PKSYAAGQLK HGPYALIDEN MPVIVIAPHD RFFDKTVTNM QEVARGGRII
     LITDEKGAAA SKLDTMHTIV LPEVDEIIAP MIFSLPLQLL AYHTAVFMGT DVDQPRNLAK
     SVTVE