(data stored in ACNUC13767 zone)

HOGENOM: BOPAR1_1_PE3979

ID   BOPAR1_1_PE3979                      STANDARD;      PRT;   610 AA.
AC   BOPAR1_1_PE3979; Q7W334;
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   (BOPAR1_1.PE3979) [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=BPP4214;
OS   BORDETELLA PARAPERTUSSIS 12822.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOPAR1_1.PE3979.
CC       Bordetella parapertussis 12822, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:GLMS_BORPA
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; Q7W334; -.
DR   EMBL; BX640436; CAE39493.1; -; Genomic_DNA.
DR   RefSeq; NP_886345.1; NC_002928.3.
DR   ProteinModelPortal; Q7W334; -.
DR   SMR; Q7W334; 2-610.
DR   GeneID; 1666708; -.
DR   GenomeReviews; BX470249_GR; BPP4214.
DR   KEGG; bpa:BPP4214; -.
DR   OMA; YWFEALA; -.
DR   PhylomeDB; Q7W334; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; BPAR257311:BPP4214-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; 1.
DR   Pfam; PF01380; SIS; 2.
DR   TIGRFAMs; TIGR01135; GlmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
DR   HOGENOMDNA; BOPAR1_1.PE3979; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
SQ   SEQUENCE   610 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIVGAVAQ RDITPILIEG LKRLEYRGYD SCGVALYMDG HLRRTRSTKR VAELSEQVAE
     DKLGGFTGIA HTRWATHGIP ATYNAHPHFS AQGKDEPRIA LVHNGIIENH EELRQELQGV
     GYVFESQTDT EVIAHLVNHL YAGDLFEAVQ QAVRRLQGAY AIAVFCRDEP HRVVGARQGS
     PLVVGLGQNE NFLASDALAL AGTTDQIIYL EDGDVVDLQL ARVWIVDQAG KQVERKAHTV
     QVHTGAAELG PYRHFMQKEI FEQPRAVGDT LQDIESITPE LFGDGAYKVF KEIDSLLILA
     CGTSYYAGLT AKYWIESIAR IPVAVEIASE YRYRDSVPNP NALVVTISQS GETADTLAAL
     KHARSLGMQH TLTVCNVATS AMVRECELAY ITRAGVEIGV ASTKAFTTQL TALFLLTLAL
     AQTRGRLTEE QEAEHLKALR HLPAAIGAVL ALEPQIMAWA DRFASKENAL FLGRGMHYPI
     ALEGALKLKE ISYIHAEAYP AGELKHGPLA LVTEHMPVVT IAPKDALLEK LKSNMQEVRA
     RGGELYVFAD ADSKIANAEG MHVIRMPEYY GALSPIVHTI PLQLLSYHTA CVRGTDVDKP
     RNLAKSVTVE
//

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