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Database: UniProt
Entry: Q4L836_STAHJ
LinkDB: Q4L836_STAHJ
Original site: Q4L836_STAHJ 
ID   Q4L836_STAHJ            Unreviewed;       601 AA.
AC   Q4L836;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 134.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, 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:BAE04189.1};
GN   OrderedLocusNames=SH0880 {ECO:0000313|EMBL:BAE04189.1};
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE04189.1, ECO:0000313|Proteomes:UP000000543};
RN   [1] {ECO:0000313|EMBL:BAE04189.1, ECO:0000313|Proteomes:UP000000543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE04189.1,
RC   ECO:0000313|Proteomes:UP000000543};
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC       {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, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001031, 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}.
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DR   EMBL; AP006716; BAE04189.1; -; Genomic_DNA.
DR   RefSeq; WP_011275192.1; NC_007168.1.
DR   AlphaFoldDB; Q4L836; -.
DR   KEGG; sha:SH0880; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_7_1_9; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 106547at2; -.
DR   Proteomes; UP000000543; 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   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00714; GFAT; 1.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GFAT.
DR   InterPro; IPR047084; GFAT_N.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   NCBIfam; TIGR01135; glmS; 1.
DR   PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR   PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00164}.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   DOMAIN          2..218
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          284..426
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          453..591
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   ACT_SITE        596
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   601 AA;  65931 MW;  963D638BBA1F4BF9 CRC64;
     MCGIVGYIGY DNAKELLLSG LEKLEYRGYD SAGIAVANDN GTTVFKEKGR IAELRKVADN
     NDTDGHVGIG HTRWATHGVP STVNSHPHQS NNERFTLVHN GVIENYEELK SEYLSDVTFQ
     SETDTEVIVQ LVEHFSNKGL ETEEAFSKVV SLLHGSYALG LLDNQDSDTI YVAKNKSPLL
     VGVGEGFNVI ASDALAMIKV TNEYKEIHDH EIVIVKKDSV TIKDLDGNVQ DRDTYTAQID
     ASDAEKGIYD HYMLKEINEQ PAVMRRIIQE YEDEKGDLKI DPEIVKDVAA ADRIYIIAAG
     TSYHAGLVGK EYLEKWAGVP TEVHVASEFV YNMPLLSEKP LFIYISQSGE TADSRAVLVE
     TNKLGYKSLT VTNVAGSTLS READHTLLLH AGPEIAVAST KAYTAQIAVL SILSQVVAKA
     HGRDNDIDLL RELAKVTTAI ETIVDDTPVM EQIAKDFLET TRNAFFIGRT MDYNVSLEGS
     LKLKEISYIQ AEGFAGGELK HGTIALIEDG TPVIALSTQE KVNLSIRGNV KEVVARGAKP
     CIISMEGLEK EGDTYVIPHV HELLTPLVSV VTLQLIAYYA ALHRGLDVDK PRNLAKSVTV
     E
//
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