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Database: UniProt
Entry: P72720
LinkDB: P72720
Original site: P72720 
ID   GLMS_SYNY3              Reviewed;         631 AA.
AC   P72720;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   29-OCT-2014, entry version 98.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164};
GN   OrderedLocusNames=sll0220;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L-
CC       glutamate + D-glucosamine 6-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00164}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SIMILARITY: Contains 2 SIS domains. {ECO:0000255|HAMAP-
CC       Rule:MF_00164}.
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DR   EMBL; BA000022; BAA16727.1; -; Genomic_DNA.
DR   PIR; S74575; S74575.
DR   RefSeq; NP_440047.1; NC_000911.1.
DR   RefSeq; YP_005650104.1; NC_017277.1.
DR   RefSeq; YP_007449930.1; NC_020286.1.
DR   ProteinModelPortal; P72720; -.
DR   STRING; 1148.sll0220; -.
DR   MEROPS; C44.971; -.
DR   PaxDb; P72720; -.
DR   EnsemblBacteria; BAA16727; BAA16727; BAA16727.
DR   GeneID; 953346; -.
DR   KEGG; syn:sll0220; -.
DR   KEGG; syy:SYNGTS_0151; -.
DR   KEGG; syz:MYO_11500; -.
DR   PATRIC; 23837172; VBISynSp132158_0161.
DR   eggNOG; COG0449; -.
DR   HOGENOM; HOG000258896; -.
DR   InParanoid; P72720; -.
DR   KO; K00820; -.
DR   OMA; SVFETQT; -.
DR   OrthoDB; EOG6KT2Q1; -.
DR   PhylomeDB; P72720; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR000583; GATase_dom.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF00310; GATase_2; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; SSF56235; 1.
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; Reference proteome; Repeat; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000255|HAMAP-
FT                                Rule:MF_00164}.
FT   CHAIN         2    631       Glutamine--fructose-6-phosphate
FT                                aminotransferase [isomerizing].
FT                                /FTId=PRO_0000135399.
FT   DOMAIN        2    225       Glutamine amidotransferase type-2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00164}.
FT   DOMAIN      298    446       SIS 1. {ECO:0000255|HAMAP-Rule:MF_00164}.
FT   DOMAIN      480    621       SIS 2. {ECO:0000255|HAMAP-Rule:MF_00164}.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00164}.
FT   ACT_SITE    626    626       For Fru-6P isomerization activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00164}.
SQ   SEQUENCE   631 AA;  69607 MW;  A681521E28918FA6 CRC64;
     MCGIVGYIGT QTAVNILIEG LERLEYRGYD SAGIATVTEG KIESVRAKGK LFNLKEKLEN
     HSNFSRLGIG HTRWATHGKP EEHNAHPHLD NQQRIAVVQN GIIENYQTLR DQLKEKGYQF
     YSETDTEVIP ILIADILKDL PSDDPDEALL EAIGKAVHQL EGAFAIAVLD AHCPEQLIVA
     RQQAPLILGF GQGEFFCASD VTALVHHTTT VLSLENGEIA RLTPLGVEVY DFNLKRVRKL
     PRTLDWSATT VEKQGFRHFM LKEIYEQPAV VRTCLATYLN EQWRAADHPS HSPVFLGLDP
     QLTKNLQHIQ VLACGTSWHA GLVGKYLLEQ LAGIPTTVHY ASEFRYAAPP LTPHTLTIGV
     TQSGETADTL AALEMEKQRR LTLEDDYKPL ILGITNRPES TLATMVNEII NTHAGIEIGV
     AATKTFVAQV LAFYFLALDI AFQRHSLSLE AIEHIMVGLR QLPAQIETIL EQQGSAIEAL
     AHEFAETQDF IFLGRGINFP IALEGALKLK EISYIHAEGY PAGEMKHGPI ALLDAKVPVV
     AIAMPGSVHD KVISNAQEAK ARDARLIGVT PMDDSQARSV FDDLLLVPHV EEMLSPIVAV
     IPLQLLSYHI AARRGLDVDQ PRNLAKSVTV E
//
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