NODM_RHIME
ID NODM_RHIME Reviewed; 608 AA.
AC Q92ZK3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 114.
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=RA0482; ORFNames=SMa0878;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Involved in the production of the root hair deformation (HAD)
CC factor specifically on medicago. {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; AE006469; AAK65140.1; -; Genomic_DNA.
DR PIR; B95322; B95322.
DR RefSeq; NP_435728.1; NC_003037.1.
DR RefSeq; WP_010967462.1; NC_003037.1.
DR AlphaFoldDB; Q92ZK3; -.
DR SMR; Q92ZK3; -.
DR EnsemblBacteria; AAK65140; AAK65140; SMa0878.
DR GeneID; 61599283; -.
DR KEGG; sme:SMa0878; -.
DR PATRIC; fig|266834.11.peg.492; -.
DR HOGENOM; CLU_012520_5_2_5; -.
DR OMA; RECALQF; -.
DR Proteomes; UP000001976; Plasmid pSymA.
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; 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_0000135437"
FT DOMAIN 2..217
FT /note="Glutamine amidotransferase type-2"
FT DOMAIN 281..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; 65919 MW; 91BC90051FEC23F4 CRC64;
MCGIVGIVGN QPVSERLVEA LKRLEYRGYD SAGVATIDAG TLQRRRAEGK LVNLESRLRE
EPLAGTIGIA HTRWATHGAP TERNAHPHFT EGVAVVHNGI IENFAELKDE LAAGGAEFQT
ETDTEVVAHL LTKYRRDGLG RREAMHAMLK RVKGAYALAV LFEDDPSTIM AARNGPPLAI
GHGSGEMFLG SDAIALAPFT NEITYLIDGD WAVIGKTGVH IFDFDGNVVE RPRQISTAAA
FLVDKGNHRH FMEKEIYEQP EVIAHALGHY VNFIENRVVP ISDAIDFGKV PSLAISACGT
AYLAGLIGKY WFERYARLPV EIDVASEFRY REIPLSPQSA ALFISQSGET ADTLASLRYC
KEHGLKIGAV VNARESTIAR ESDAVFPILA GPEIGVASTK AFTCQLAVLA ALAVGAGKAR
GTISGEEEQA LVKSLAEMPR IMGQVLNSIQ PKIESLSREL SKCHDVLYLG RGTSFPLAME
GALKLKEISY IHAEGYAAGE LKHGPIALID ENMPVIVIAP HDRFFDKTVS NMQEVAARGG
RIILITDEKG AAASKLDTMH TIVLPEVDEI IAPMIFSLPL QLLAYHTAVF MGTDVDQPRN
LAKSVTVE
