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Database: UniProt
Entry: Q8PCY1
LinkDB: Q8PCY1
Original site: Q8PCY1 
ID   GLMS_XANCP              Reviewed;         609 AA.
AC   Q8PCY1;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   01-OCT-2014, entry version 81.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164};
GN   OrderedLocusNames=XCC0569;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 /
OS   LMG 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L-
CC       glutamate + D-glucosamine 6-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00164}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SIMILARITY: Contains 2 SIS domains. {ECO:0000255|HAMAP-
CC       Rule:MF_00164}.
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DR   EMBL; AE008922; AAM39885.1; -; Genomic_DNA.
DR   RefSeq; NP_635961.1; NC_003902.1.
DR   ProteinModelPortal; Q8PCY1; -.
DR   SMR; Q8PCY1; 2-609.
DR   STRING; 190485.XCC0569; -.
DR   MEROPS; C44.971; -.
DR   EnsemblBacteria; AAM39885; AAM39885; XCC0569.
DR   GeneID; 1001073; -.
DR   KEGG; xcc:XCC0569; -.
DR   PATRIC; 24071781; VBIXanCam115730_0626.
DR   eggNOG; COG0449; -.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; HIINTLA; -.
DR   OrthoDB; EOG6KT2Q1; -.
DR   BioCyc; XCAM190485:GIXZ-569-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; Reference proteome; Repeat; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000255|HAMAP-
FT                                Rule:MF_00164}.
FT   CHAIN         2    609       Glutamine--fructose-6-phosphate
FT                                aminotransferase [isomerizing].
FT                                /FTId=PRO_0000135415.
FT   DOMAIN        2    217       Glutamine amidotransferase type-2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00164}.
FT   DOMAIN      284    425       SIS 1. {ECO:0000255|HAMAP-Rule:MF_00164}.
FT   DOMAIN      458    599       SIS 2. {ECO:0000255|HAMAP-Rule:MF_00164}.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00164}.
FT   ACT_SITE    604    604       For Fru-6P isomerization activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00164}.
SQ   SEQUENCE   609 AA;  66094 MW;  9E88C6881020F490 CRC64;
     MCGIVGAIAG RDVVPVLIEG LKRLEYRGYD SSGIAVLDGT QVRRVRRTGR VAEMAQAAQA
     EQFGATLGIG HTRWATHGGV TEANAHPHIS AGVALVHNGI IENHEEQREK LRALGYTFES
     QTDTEVIAHL IHHHLADAGD LLSALQRTVK ELTGAYALAV MSQAEQERFV CARMGCPLLI
     GVGEGENFVA SDVSAIVQAT RQVIFLEEGD TAELRRDGVR VFDASDAAVE RPLHLSDVSL
     ASLELGPFRH FMQKEIHEQP RALADTIEAA IDAKGFPASL FGPTADAVLR DIEGVQILAC
     GTSYYAGLTA RYWIEAIAGL PCSVEIASEY RYRAAYANPK HLIVTISQSG ETLDTMEALK
     YAKSLGHLHT LSICNVPESA IPRASELVCY TRAGAEIGVA STKAFTTQLA VLFQLTMVLG
     KLQGRISDSE EADYLEQLRF LPGSVQHALN LEPQIMAWAE RFSPKENALF LGRGLHYPIA
     LEGALKLKEI SYIHAEAYPA GELKHGPLAL VDATMPVVVI APNDRLLEKV KSNMQEVRAR
     GGELFVFADQ DSHFSESDGV HVIRTPRHAG VLSPVIHTIP VQLLAYHTAL ARGTDVDKPR
     NLAKSVTVE
//
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