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 09-APR-2025, entry version 110.
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; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; 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:0005829; C:cytosol; IEA:TreeGrafter.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:TreeGrafter.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:TreeGrafter.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:TreeGrafter.
DR CDD; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR FunFam; 3.40.50.10490:FF:000001; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 1.
DR FunFam; 3.40.50.10490:FF:000002; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 1.
DR FunFam; 3.60.20.10:FF:000006; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 1.
DR Gene3D; 3.40.50.10490; Glucose-6-phosphate isomerase like protein, domain 1; 2.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR005855; GFAT.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR01135; glmS; 1.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53697; SIS domain; 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
//