(data stored in SCRATCH zone)

SWISSPROT: A5GQ78_SYNR3

ID   A5GQ78_SYNR3            Unreviewed;       628 AA.
AC   A5GQ78;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS00887593};
DE            EC=2.6.1.16 {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164,
GN   ECO:0000313|EMBL:CAK27037.1};
GN   OrderedLocusNames=SynRCC307_0134 {ECO:0000313|EMBL:CAK27037.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27037.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27037.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725,
CC         ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00164};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
CC       ECO:0000256|SAAS:SAAS00887591}.
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DR   EMBL; CT978603; CAK27037.1; -; Genomic_DNA.
DR   RefSeq; WP_011934552.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0134; -.
DR   MEROPS; C44.A08; -.
DR   EnsemblBacteria; CAK27037; CAK27037; SynRCC307_0134.
DR   KEGG; syr:SynRCC307_0134; -.
DR   eggNOG; ENOG4105C46; Bacteria.
DR   eggNOG; COG0449; LUCA.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 43416at2; -.
DR   BioCyc; SSP316278:G1GJL-134-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 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;
DR   PRODOM; A5GQ78.
DR   SWISS-2DPAGE; A5GQ78.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:CAK27037.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000256|SAAS:SAAS00887588};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:CAK27037.1}.
FT   INIT_MET      1      1       Removed. {ECO:0000256|HAMAP-Rule:
FT                                MF_00164}.
FT   DOMAIN        2    228       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   DOMAIN      296    445       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   DOMAIN      479    618       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
FT   ACT_SITE    623    623       For Fru-6P isomerization activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
SQ   SEQUENCE   628 AA;  67185 MW;  2F6B182E0107A5EC CRC64;
     MCGIVAVIGT RDAAPLLLDG LRQLEYRGYD SAGIATVHGG HLSHLRAEGK LINLTQRFEA
     SGAAGSCGIG HTRWATHGKP EERNAHPHLD GSGELAVVQN GIIENHRSLR ERLAAGGAAF
     QSDTDTEVIP HLVSQELKGL LAAGSPADGA TLLKAVQQAL PQLDGAYALA VVWAQCPDAL
     VVARRQAPLL IGFGEGEFLC ASDTPALAGV TRTILPLEDG EVALLGPLGI ELYNEAGERQ
     QRPPTQLQGT DHVADKRSFR HFMLKEIHEQ PETAARWLLR HLPEGGPNDP LVALPLERSL
     LEGVQRIQIL ACGTSRHAAL VGAHLLEQLA GIPTSVHYAS EFRYSPPPLA PHTLTIGVTQ
     SGETADTLAA LAMEQQRCAD HGDPAYAARL LGITNRTESS LGRLVPQLID IAAGVEVGVA
     ATKTFLGQLL AFYGLAIQLT DLRGARSREQ LHPLLAELRA LPAQLQTLID RLDLRCAELA
     HAFADTRTVI YLGRGINYPI ALEGALKLKE ISYIHAEGYP AGEMKHGPIA LLDADVPVVS
     VAMPGPVFDK VLSNAQEAKA RDARLIGVAP ECPDTEIFDE LLPVPAVDEL LSPLLTLIPM
     QLLSYHIAAR RGLDVDQPRN LAKSVTVE
//

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