NODM_BRADU
ID NODM_BRADU Reviewed; 608 AA.
AC P94323;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 130.
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; OrderedLocusNames=blr1632;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-608.
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=9612946; DOI=10.1094/mpmi.1998.11.6.476;
RA Lohrke S.M., Day B., Kolli V.S., Hancock R., Yuen J.P., de Souza M.L.,
RA Stacey G., Carlson R., Tong Z., Hur H.G., Orf J.H., Sadowsky M.J.;
RT "The Bradyrhizobium japonicum noeD gene: a negatively acting, genotype-
RT specific nodulation gene for soybean.";
RL Mol. Plant Microbe Interact. 11:476-488(1998).
CC -!- FUNCTION: Involved in the production of the root hair deformation (HAD)
CC factor specifically on soybean. {ECO:0000250}.
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; BA000040; BAC46897.1; -; Genomic_DNA.
DR EMBL; U67278; AAB39494.1; -; Genomic_DNA.
DR RefSeq; NP_768272.1; NC_004463.1.
DR RefSeq; WP_011084447.1; NZ_CP011360.1.
DR AlphaFoldDB; P94323; -.
DR SMR; P94323; -.
DR STRING; 224911.27349884; -.
DR EnsemblBacteria; BAC46897; BAC46897; BAC46897.
DR GeneID; 64021485; -.
DR KEGG; bja:blr1632; -.
DR PATRIC; fig|224911.44.peg.1076; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_5; -.
DR InParanoid; P94323; -.
DR OMA; TSYYSGC; -.
DR PhylomeDB; P94323; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
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 Reference proteome; 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_0000135434"
FT DOMAIN 2..217
FT /note="Glutamine amidotransferase type-2"
FT DOMAIN 284..423
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"
FT CONFLICT 331
FT /note="Y -> N (in Ref. 2; AAB39494)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..341
FT /note="PLRRGDL -> LAPRQF (in Ref. 2; AAB39494)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="S -> L (in Ref. 2; AAB39494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 65390 MW; 32C12A4AB7FD1D76 CRC64;
MCGIVGILGR GPVVDKLVAS LRRLEYRGYD SAGLATLEGV RIERRRAEGK LRNLEEQLRY
CPPSGHAGIG HTRWATHGKP TESNAHPHAT ENVAVVHNGI IENFRELRAE LERNGAGFNS
ETDTEVVAHL VDSYLKNGYS PQDAVQASLP RLRGAFALAF LFKANDDLLI GACKGSPLAI
GHGRGEVYLG SDAIALAPLT DTVTYLEDGD WAVLTRATCV IYGADGSIVQ RETSKSGVSA
LLVDKANYRH FMAKEIHEQP TVAGKTLAHY LDVAAKRVAL PLALPFDFNC IQRISITACG
TASYAGHIAK YWFERLARLP CDVDVASEFR YREAPLRRGD LAIVISQSGE TADTLAALRY
AKGKGLHTIS VVNVPTSTIA RESESVLPTL AGPEIGVAST KAFICQLMVL GVLAVRAAKE
RGKLSEIDES QLVRELIEVP RLIAAALLVE PQIEKLARYI AGARTVLYLG RGTSAPLALE
GALKLKEISY IHSEGYAAGE LKHGPIALID EAVPVVVIAP YDEVFEKTVS NMQEVAARGG
KIILITDAKG ASEAMVDTLL TIVLPAMVAS FTPLVYAIPV QLLAYHTAVA RGADVDQPRN
LAKSVTVE
