(data stored in ACNUC13767 zone)

HOGENOM: CHTEP1_1_PE130

ID   CHTEP1_1_PE130                       STANDARD;      PRT;   614 AA.
AC   CHTEP1_1_PE130; Q8KG38;
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   (CHTEP1_1.PE130) [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=CT0130;
OS   CHLOROBIUM TEPIDUM TLS.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHTEP1_1.PE130.
CC       Chlorobium tepidum TLS, complete genome.
CC       1..43554 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:GLMS_CHLTE
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; Q8KG38; -.
DR   EMBL; AE006470; AAM71378.1; -; Genomic_DNA.
DR   RefSeq; NP_661036.1; NC_002932.3.
DR   ProteinModelPortal; Q8KG38; -.
DR   GeneID; 1006837; -.
DR   GenomeReviews; AE006470_GR; CT0130.
DR   KEGG; cte:CT0130; -.
DR   NMPDR; fig|194439.1.peg.130; -.
DR   TIGR; CT0130; -.
DR   OMA; LCASQES; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; CTEP194439:CT_0130-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; CHTEP1_1.PE130; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Reference proteome; Repeat; Transferase.
SQ   SEQUENCE   614 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIIGYIGR REAAPLLLNG LKRLEYRGYD SAGMAVLNGS MKMLKKKGSV SNLEELLNVS
     GTVMLGATVG IAHTRWATHG DPSDRNAHPH MNVSGDIALI HNGIIENYSA LKQELMGEGY
     VFESDTDSEV LVHLIDRIWK NDSALGLEGA VRQALRHVEG AYGICVVSSR EPDKIVVARK
     GSPLVIGLGD GEFFIASDAA PIVEHTNKVV YLSDGEMAVV TRDSYTVKTI ENVEQQKRVT
     ELDFSLEKIE KGGFEHFMLK EIFEQPEVMR DVMRGRVRVE EGRVHLGGIH DYLDRLKQAK
     RIMICACGTS WHAGLIGEYL IEEFARIPVE VDYASEFRYR NPIVSSDDVV IVISQSGETA
     DTLAALRLAK EKGAMVMGIC NVVGSTIPRE TLCGMYTHAG PEVGVASTKA FTAQVIVLFM
     LAMALSKGRT ISQEEIKLNL RELAEVPDKV AWILEQNDAI KEIAVKLKDA RNALYLGRGY
     NFPVALEGAL KLKEISYIHA EGYPAAEMKH GPIALIDEDM PVIVIATRDN TYAKILSNIE
     EVRSRKGRVI AIASEGDREI ERLTEDVIYI PQASAAVLPL LTVIPLQLLS YHVATLRGCN
     VDRPRNLAKS VTVE
//

If you have problems or comments...

PBIL Back to PBIL home page