(data stored in ACNUC13767 zone)

HOGENOM: PSSYR1_1_PE5461

ID   PSSYR1_1_PE5461                      STANDARD;      PRT;   611 AA.
AC   PSSYR1_1_PE5461; Q87TT8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glucosamine--fructose-6-phosphate aminotransferase
DE   (PSSYR1_1.PE5461) [isomerizing]; EC=2.6.1 16;AltName:
DE   Full=D-fructose-6-phosphate amidotransferase;AltName: Full=GFAT;AltName:
DE   Full=Glucosamine-6-phosphate synthase;AltName: Full=Hexosephosphate
DE   aminotransferase;AltName: Full=L-glutamine-D-fructose-6-phosphate
DE   amidotransferase; .
GN   Name=glmS; OrderedLocusNames=PSPTO_5595;
OS   PSEUDOMONAS SYRINGAE PV. TOMATO STR. DC3000.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PSSYR1_1.PE5461.
CC       Pseudomonas syringae pv. tomato str. DC3000 chromosome, complete genome
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:GLMS_PSESM
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.
CC   -!- SIMILARITY: Contains 2 SIS domains.
CC   -!- GENE_FAMILY: HOG000258898 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q87TT8; -.
DR   EMBL; AE016853; AAO59008.1; -; Genomic_DNA.
DR   RefSeq; NP_795313.1; NC_004578.1.
DR   ProteinModelPortal; Q87TT8; -.
DR   SMR; Q87TT8; 2-611.
DR   GeneID; 1187287; -.
DR   GenomeReviews; AE016853_GR; PSPTO_5595.
DR   KEGG; pst:PSPTO_5595; -.
DR   NMPDR; fig|223283.1.peg.5451; -.
DR   TIGR; PSPTO_5595; -.
DR   OMA; YWFEALA; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; PSYR223283:PSPTO_5595-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:EC.
DR   GO; GO:0005529; F:sugar binding; IEA:InterPro.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00164; GlmS; 1; -.
DR   InterPro; IPR000583; GATase_2.
DR   InterPro; IPR017932; GATase_II.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR001347; SIS.
DR   Pfam; PF00310; GATase_2; 2.
DR   Pfam; PF01380; SIS; 2.
DR   TIGRFAMs; TIGR01135; GlmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
DR   HOGENOMDNA; PSSYR1_1.PE5461; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
SQ   SEQUENCE   611 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIVGAVAE RNITAILLEG LKRLEYRGYD SAGVAVFTNE GVLERRRRSG KVSELEQALA
     GEPLIGRLGI AHTRWATHGA PCERNAHPHF SADELAVVHN GIIENHEALR EQLKSLGYVF
     VSDTDTEVIV HLLHHKLKDT PDLAVALKSA VKELHGAYGL AVINAAQPDR LLAARSGSPL
     VIGVGMGENF LASDQLALRQ VTDRFMYLEE GDIAEIRRDS VQIWTVDGLP VVREVVQYHE
     GAEAADKGEY RHFMLKEIHE QPKVVQRTLE GRLGQHQVLV HAFGPQAAEL FAKVRNVQIV
     ACGTSYHAGM VARYWLEGLA GIPCQVEVAS EFRYRKVVVQ PDTLFVSISQ SGETADTLAA
     LRNAKELGFL ASLAICNVGI SSLVRESDLT LLTQAGPEIG VASTKAFTTQ LVALLLLTLS
     LGQVKGSLEE GVEAQLVEEL RRLPTRLGEA LAMDGTIEKV AELFAEKHHT LFLGRGAQFP
     VAMEGALKLK EISYIHAEAY PAGELKHGPL ALVDADMPVV TVAPNNELLE KLKSNLQEVR
     ARGGELIVFA DEQAGMKNGE GTHVIAMPHI IDALAPILYT IPLQLLSYYV AVLKGTDVDQ
     PRNLAKSVTV E
//

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