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Database: UniProt
Entry: O57981
LinkDB: O57981
Original site: O57981 
ID   GLMS_PYRHO              Reviewed;         598 AA.
AC   O57981;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   19-FEB-2014, entry version 92.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE            EC=2.6.1.16;
DE   AltName: Full=D-fructose-6-phosphate amidotransferase;
DE   AltName: Full=GFAT;
DE   AltName: Full=Glucosamine-6-phosphate synthase;
DE   AltName: Full=Hexosephosphate aminotransferase;
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN   Name=glmS; OrderedLocusNames=PH0243;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 /
OS   NBRC 100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA29315.1; Type=Erroneous initiation;
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DR   EMBL; BA000001; BAA29315.1; ALT_INIT; Genomic_DNA.
DR   PIR; D71248; D71248.
DR   RefSeq; NP_142239.1; NC_000961.1.
DR   ProteinModelPortal; O57981; -.
DR   STRING; 70601.PH0243; -.
DR   MEROPS; C44.971; -.
DR   PRIDE; O57981; -.
DR   EnsemblBacteria; BAA29315; BAA29315; BAA29315.
DR   GeneID; 1444133; -.
DR   KEGG; pho:PH0243; -.
DR   eggNOG; COG0449; -.
DR   HOGENOM; HOG000258898; -.
DR   KO; K00820; -.
DR   OMA; CVISERE; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; PHOR70601:GJWR-234-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR001347; SIS.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    598       Glutamine--fructose-6-phosphate
FT                                aminotransferase [isomerizing].
FT                                /FTId=PRO_0000135431.
FT   DOMAIN        2    219       Glutamine amidotransferase type-2.
FT   DOMAIN      280    420       SIS 1.
FT   DOMAIN      449    588       SIS 2.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity (By
FT                                similarity).
FT   ACT_SITE    593    593       For Fru-6P isomerization activity (By
FT                                similarity).
SQ   SEQUENCE   598 AA;  66110 MW;  3A8DD0466416544D CRC64;
     MCGIIGYIGP RKASDVIVEG LKRLEYRGYD SAGIATCYEG KIFIKKGAGK IDELVKKLNF
     LELPGNIGIG HTRWATHGIP NDTNAHPHTD CTGKIVVVHN GIIENFQELK RELLKRGHVF
     RSDTDTEVIA HLIEENLRIT GNFEDAFRMS LLRLRGSYAL VVLFADDPER LYIARKDSPL
     IIGIGKGEMF MASDIPAFLA YTRRAVFLDD GEYGIVSKDW FTIKDIITGA VKTKEIHEIQ
     WTLEMAEKGG YEHFMLKEIF EQPKAIKDAI YGNVKEAPKV AELLMKYDRI IITGMGTSYH
     AALVGKYLIQ RFGKVPVIVE EASELRYEYE DILDNRSLLI AITQSGETAD TVAAMKLAKS
     KGVEVVGIVN VVGSLATRIA DETLYTHAGP EIGVAATKTY TTQLVVLTLL AKELGKLVGI
     DVSQIEGTIP RLPELVDSSL KINDKIREIA VKLNDKRDFF YIGRGINYPT ALEGALKIKE
     IAYVHAEGLS AGELKHGPLA LIEDGIPVVG IAPTGKTFEK MLSNIEEAKA RGGFIISLGD
     DVRLHQVSDI FIRLPKVPEE LAPITYIVPL QLLAYHLAVL KGHNPDRPRN LAKSVTVE
//
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