GenomeNet

Database: UniProt
Entry: H8GRE4_METAL
LinkDB: H8GRE4_METAL
Original site: H8GRE4_METAL 
ID   H8GRE4_METAL            Unreviewed;       610 AA.
AC   H8GRE4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
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   ORFNames=Metal_3474 {ECO:0000313|EMBL:EIC31123.1};
OS   Methylomicrobium album BG8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomicrobium.
OX   NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC31123.1, ECO:0000313|Proteomes:UP000005090};
RN   [1] {ECO:0000313|EMBL:EIC31123.1, ECO:0000313|Proteomes:UP000005090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BG8 {ECO:0000313|EMBL:EIC31123.1,
RC   ECO:0000313|Proteomes:UP000005090};
RX   PubMed=23580712;
RA   Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., Op den Camp H.J.,
RA   Vuilleumier S., Bringel F., Dispirito A.A., Murrell J.C., Bruce D.,
RA   Cheng J.F., Copeland A., Goodwin L., Hauser L., Lajus A., Land M.L.,
RA   Lapidus A., Lucas S., Medigue C., Pitluck S., Woyke T., Zeytun A.,
RA   Stein L.Y.;
RT   "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph
RT   Methylomicrobium album Strain BG8.";
RL   Genome Announc. 1:E0017013-E0017013(2013).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001475; EIC31123.1; -; Genomic_DNA.
DR   RefSeq; WP_005374235.1; NZ_CM001475.1.
DR   AlphaFoldDB; H8GRE4; -.
DR   STRING; 686340.Metal_3474; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_6; -.
DR   Proteomes; UP000005090; 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   Reference proteome {ECO:0000313|Proteomes:UP000005090};
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          286..426
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          458..600
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        605
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   610 AA;  66753 MW;  9D4614E311D67ED9 CRC64;
     MCGIVGGVVK SNLVPILMDG LKKLEYRGYD SAGLAVIGEQ GICCKRMQGK VKNLQDLLDE
     DPISGCTGIA HTRWATHGKP SSENAHPHIC RNKIAVVHNG IIENYRQLQE QQLKNGYVFA
     SETDTEVIVN EIFDALRHTD GLLNAVKRSI PKFEGTYALG IMSNDEPGLL VACRQGSPLV
     IGVGAGEYFI ASDVAALLPV TQRFIFLENG DIAAIRQSGV TVFDRNGRKA VRPVKESLLT
     ADSIEKGEYR HFMLKEIFEQ SFAVARTLQG RFVDNRLQES AFGRRAAEIF DAVRAVQIVA
     CGTSYHAGLI ARYWLERLAR IPCSVEIASE FRYREPILGP DTLAVAISQS GETADTLAAL
     QEAKKRGAKY SLAICNVPES SLVREADAVL MTRAGPEIGV ASTKAFTSQL TVSMLLVIAL
     GRRFGLSEAL ERQITAELFN LPAEIEKVLQ LNDEIKNLAR QFTEKHHALF LGRGSHYPIA
     LEGALKLKEI SYIHAEAYPA GELKHGPLAL IDAGMPVVTV APNDHMLEKL KANMEEVSAR
     DGQLIVFIDE RLASAVEAGN FKIIKVPQVE NHLSPAVYNI PLQLLSYHVA ALKGTDIDQP
     RNLAKSVTVE
//
DBGET integrated database retrieval system