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Database: UniProt/TrEMBL
Entry: A9VXX2_METEP
LinkDB: A9VXX2_METEP
Original site: A9VXX2_METEP 
ID   A9VXX2_METEP            Unreviewed;       608 AA.
AC   A9VXX2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   11-JUN-2014, entry version 49.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE            EC=2.6.1.16;
DE   AltName: Full=D-fructose-6-phosphate amidotransferase;
DE   AltName: Full=GFAT;
DE   AltName: Full=Glucosamine-6-phosphate synthase;
DE   AltName: Full=Hexosephosphate aminotransferase;
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN   Name=glmS; OrderedLocusNames=Mext_4157;
OS   Methylobacterium extorquens (strain PA1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L-
CC       glutamate + D-glucosamine 6-phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
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DR   EMBL; CP000908; ABY32526.1; -; Genomic_DNA.
DR   RefSeq; YP_001641597.1; NC_010172.1.
DR   ProteinModelPortal; A9VXX2; -.
DR   STRING; 419610.Mext_4157; -.
DR   EnsemblBacteria; ABY32526; ABY32526; Mext_4157.
DR   GeneID; 5833122; -.
DR   KEGG; mex:Mext_4157; -.
DR   PATRIC; 22538975; VBIMetExt98426_4226.
DR   eggNOG; COG0449; -.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; QVISWSE; -.
DR   OrthoDB; EOG6KT2Q1; -.
DR   BioCyc; MEXT419610:GI32-4213-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
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; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   DOMAIN        2    217       Glutamine amidotransferase type-2 (By
FT                                similarity).
FT   ACT_SITE      2      2       Nucleophile; for GATase activity (By
FT                                similarity){EA2}.
FT   ACT_SITE    603    603       For Fru-6P isomerization activity (By
FT                                similarity){EA2}.
SQ   SEQUENCE   608 AA;  65231 MW;  52052BDF81BC1F59 CRC64;
     MCGIVGIVGR ESVADALVEA LRRLEYRGYD SAGIATLDHG RLDRRRAEGK LSNLQLKLAQ
     APLPGAIGIG HTRWATHGRP NETNAHPHAT ERLAVVHNGI IENFRELKSE LEAAGARFES
     ETDTEVVAQL VSHLMEQGLG PVAAVEAALP RLHGAFALAF LFAGEDDFLI GARHGAPLAI
     GFGQGETYLG SDALALAPFT DQITYLEEGD WAILTRDGAE IRDITGAVVR RPRQRIATQA
     FLVDKGNHRH FMAKEIHEQP EVVGRTLANY VDMARGQVVL REELPFDFAR LSRLSITACG
     TAYYAGLVAK YWFETLARLP VEIDVASETR YREPPLERDG LTLVISQSGE TADTLASLRY
     AKAQGQHTLA VVNVPTSTIA RESSAVMPTF AGPEIGVAST KAFSCQLTVL LCLALAAGRA
     RGTLSAERER AVVDALITAP GLMAEAVKME AEVEGLAREI AKARDVLYLG RGTSYPMALE
     GALKLKEISY IHAEGYAAGE LKHGPIALID ESVPVIVIAP HDAIFEKTVS NMQEVAARGG
     KIILVGDAKG AAAAGLDTLA TLTMPDVDPV IAPIVYAVPI QLIAYHTAVF MGKDVDQPRN
     LAKSVTVE
//
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