(data stored in ACNUC13767 zone)

HOGENOM: PHLUM1_1_PE37

ID   PHLUM1_1_PE37                        STANDARD;      PRT;   609 AA.
AC   PHLUM1_1_PE37; Q7NA97;
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   (PHLUM1_1.PE37) [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=plu0037;
OS   PHOTORHABDUS LUMINESCENS SUBSP. LAUMONDII TTO1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PHLUM1_1.PE37.
CC       Photorhabdus luminescens subsp. laumondii TTO1, complete genome.
CC       1..3518 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:GLMS_PHOLL
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; Q7NA97; -.
DR   EMBL; BX571859; CAE12332.1; -; Genomic_DNA.
DR   RefSeq; NP_927413.1; NC_005126.1.
DR   ProteinModelPortal; Q7NA97; -.
DR   SMR; Q7NA97; 2-609.
DR   GeneID; 2799981; -.
DR   GenomeReviews; BX470251_GR; plu0037.
DR   KEGG; plu:plu0037; -.
DR   NMPDR; fig|243265.1.peg.37; -.
DR   GenoList; plu0037; -.
DR   OMA; YWFEALA; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; PLUM243265:PLU0037-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; PHLUM1_1.PE37; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
SQ   SEQUENCE   609 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIVGAVAQ RDIAEILIEG LRRLEYRGYD SAGLAVVDNE KNMFRLREVG KVQVLADEVD
     KQPVLGGTGI AHTRWATHGE PNEKNAHPHV SDYIAVVHNG IIENYEELRV QLIALGYQFI
     SDTDTEVIAH LVHWEQKQGG TLLEAIQRVI PRLRGAYGAV IMDSRDPGTI IAARSGSPLV
     IGLGVGENFL ASDQLALLPV TRRFIFLEEG DIAEVTRRTV RIFNTQGKPV EREQIESNIQ
     YDAGDKGIYR HYMQKEIYEQ PMAIKSTLER RLSHGQVDLS ELGPNAAKLL AKVEHIQIVA
     CGTSYNAGMV SRYWFEALAG IPCDVEIASE FRYRKSARRS GSLLITLSQS GETADTLAAL
     RLSKELGYLT SLTVCNVAGS SLVRESDFAL MTKAGAEIGV ASTKAFTTQL TVLLMLVAYL
     GRLKGVDAEQ EQEIVHALHA LPSRIEGMLS KDKIIEVLAE DFSDKHHALF LGRGDQYPIA
     VEGALKLKEI SYIHAEAYAA GELKHGPLAL IDADMPVIIV APNNELLEKL KSNIEEVRAR
     GGLLYVFADQ DAGFTDSEGM KIIPLPHVEE LIAPIFYTVP LQLLSYHVAL IKGTDVDQPR
     NLAKSVTVE
//

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