(data stored in ACNUC13767 zone)

HOGENOM: LEGPH_1_PE2777

ID   LEGPH_1_PE2777                       STANDARD;      PRT;   604 AA.
AC   LEGPH_1_PE2777; Q5ZRP4;
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   (LEGPH_1.PE2777) [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=lpg2836;
OS   LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR. PHILADELPHIA 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEGPH_1.PE2777.
CC       Legionella pneumophila subsp. pneumophila str. Philadelphia 1 chromosom
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:GLMS_LEGPH
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; Q5ZRP4; -.
DR   EMBL; AE017354; AAU28884.1; -; Genomic_DNA.
DR   RefSeq; YP_096831.1; NC_002942.5.
DR   ProteinModelPortal; Q5ZRP4; -.
DR   SMR; Q5ZRP4; 2-604.
DR   STRING; Q5ZRP4; -.
DR   GeneID; 3079750; -.
DR   GenomeReviews; AE017354_GR; lpg2836.
DR   KEGG; lpn:lpg2836; -.
DR   NMPDR; fig|272624.3.peg.2776; -.
DR   eggNOG; COG0449; -.
DR   OMA; YWFEALA; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; LPNE272624:LPG2836-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; LEGPH_1.PE2777; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
SQ   SEQUENCE   604 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIMGAVSE RDISKILLEG LRRLEYRGYD SAGIAVIDSQ DRLKRVRIQG KVQNLADAMQ
     ETAIAGNTGI AHTRWATHGK PSEQNAHPHL SHGEIALVHN GIIENHEHLR QQLITYGYQF
     TSETDTEVAA HLIHYHYQQH ENLLLAVQKA AAEMQGAFAL GVIHQKRPEE LVAIRKGSPL
     VLGFGIGENF IASDALALRS FAQSVIYMEE GDSACVTTQD IKVYDSNRIL VQRAVHPLNS
     DSEIVNKGPY RHFMLKEIFE QSKVITDTLE SRINSIDVLR ASFGEKASHI FPVVKNIHIV
     ACGTSYHAGM IAKYWLESLA GLPTQVEIAS EYRYRDVVVP DNTLFITVSQ SGETADTLAA
     LFKAKQSNYL ASLAICNVAT STLVREADCV FLTRAGIEIG VASTKAFTTQ LAAFLMLAAA
     LCKDNRAQEV LRQLQELPAC CERVLQMNEE VESLASLFVN KVHALFLGRG VQYPVALEGA
     LKLKEISYIH AEAYPAGELK HGPLALVDKD MPVIAVAPND ELLDKLKSNL HEVSARGGQL
     FVFVDDSQNW KANGARLIKV PSCGAWLAPI VYTIPLQLLA YHVAVAKGTD VDQPRNLAKS
     VTVE
//

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