(data stored in ACNUC13767 zone)

HOGENOM: PSEPK_1_PE5339

ID   PSEPK_1_PE5339                       STANDARD;      PRT;   611 AA.
AC   PSEPK_1_PE5339; Q88BX8;
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   (PSEPK_1.PE5339) [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=PP_5409;
OS   PSEUDOMONAS PUTIDA KT2440.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PSEPK_1.PE5339.
CC       Pseudomonas putida KT2440 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:GLMS_PSEPK
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; Q88BX8; -.
DR   EMBL; AE015451; AAN70973.1; -; Genomic_DNA.
DR   RefSeq; NP_747509.1; NC_002947.3.
DR   ProteinModelPortal; Q88BX8; -.
DR   SMR; Q88BX8; 2-611.
DR   STRING; Q88BX8; -.
DR   GeneID; 1041649; -.
DR   GenomeReviews; AE015451_GR; PP_5409.
DR   KEGG; ppu:PP_5409; -.
DR   NMPDR; fig|160488.1.peg.5339; -.
DR   TIGR; PP_5409; -.
DR   eggNOG; COG0449; -.
DR   OMA; YWFEALA; -.
DR   PhylomeDB; Q88BX8; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; PPUT160488:PP_5409-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; PSEPK_1.PE5339; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
SQ   SEQUENCE   611 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIVGAVAE RNITAILIEG LKRLEYRGYD SAGLAVLTQN GELQRRRRIG KVSELEVAVA
     DDPLAGQLGI AHTRWATHGA PTEGNAHPHF SGNDVAVVHN GIIENHEELR EELKGLGYVF
     TSQTDTEVIV HLIHHTLKSI PDLTDALKAA VKRLHGAYGL ALISAKQPDR LVAARSGSPL
     VIGLGLGENF LASDQLALRQ VTDRFMYLEE GDIAEIRRDQ VSIWDQQGNK VQRETVQYHE
     GAEAADKGAY RHFMLKEIHE QPSVVQRTLE GRLGKDNVLV QAFGPQAADL FAKVRNVQIV
     ACGTSYHAGM VARYWLESLA GIPCQVEVAS EFRYRKVVVQ PDTLFVSISQ SGETADTLAA
     LRNAKELGFL GSLAICNVGI SSLVRESDLT LLTLAGPEIG VASTKAFTTQ LVSLMLLTLA
     LGQVRGTLEA GVEAELVEEL RRLPTRLGEA LAMDATVEKI AELFADKHHT LFLGRGAQYP
     VAMEGALKLK EISYIHAEAY PAGELKHGPL ALVDNDMPVV TVAPNNELLE KLKSNLQEVR
     ARGGELVVFA DEHAGMTNGE GTHVIKVPHI ADALAPILYT IPLQLLSYYV AVLKGTDVDQ
     PRNLAKSVTV E
//

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