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Database: UniProt
Entry: B7ATA5_9FIRM
LinkDB: B7ATA5_9FIRM
Original site: B7ATA5_9FIRM 
ID   B7ATA5_9FIRM            Unreviewed;       635 AA.
AC   B7ATA5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
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=BACPEC_01375 {ECO:0000313|EMBL:EEC56889.1};
OS   [Bacteroides] pectinophilus ATCC 43243.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=483218 {ECO:0000313|EMBL:EEC56889.1, ECO:0000313|Proteomes:UP000003136};
RN   [1] {ECO:0000313|EMBL:EEC56889.1, ECO:0000313|Proteomes:UP000003136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC56889.1,
RC   ECO:0000313|Proteomes:UP000003136};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides pectinophilus (ATCC 43243).";
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEC56889.1, ECO:0000313|Proteomes:UP000003136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC56889.1,
RC   ECO:0000313|Proteomes:UP000003136};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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; ABVQ01000036; EEC56889.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7ATA5; -.
DR   STRING; 483218.BACPEC_01375; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_9; -.
DR   Proteomes; UP000003136; Unassembled WGS sequence.
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        30
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   DOMAIN          31..245
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          312..451
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          484..625
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   ACT_SITE        31
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   ACT_SITE        630
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   635 AA;  70240 MW;  4A2772C2785880C4 CRC64;
     MIHKVHKRYF LCSHANWNAQ VDVQEWRNNM CGIVGYVGRR DCADVLINAL TKLEYRGYDS
     AGIAVFENNA IRVEKSKGRL QNLVDKMKID GKPQGHVGIG HTRWATHGEP SDINSHPHGN
     KRVTIVHNGI IENYKQIKDF LIKEGYSFVS ETDTETVAKL LDYYYNGNPI ETIARVIAEI
     KGSYALGIMF RDYPDAIFAV RKECPLIAGV GEGENFIASD VPAILQYTRN YYLLEQNEIA
     IVKEDSIKIC DIHGMEINKE LQTADWDEDA AEKGGYEHFM LKEIHEQPTA VRTTITPRIV
     NGMPDFASDG IDINKLSSYR QIFIVACGTA MHAGMVGKYV IEKMARVSVT VDIASEFRYR
     DPLITDKDLV IVISQSGETA DTLAVLKLAK EMKAATLAVV NVKGSSIARE ADHVIYTHAG
     PEISVASTKA YMVQVAVMYL IAFALSRETG HITDAQCAEF TEKLKNIPAV IEEAIGLKDR
     CQFAASKLLN AESLLYIGRG LDYALSMEGS LKLKEISYIH SESYAAGELK HGTISLITEG
     MPVIAVATQK SIVEKTISNI KEVKARGAMV ILVCGKDIEV EDNVADIIIR LPEADEVLMP
     MVAAVPLQLI AYYTAVLKGC DVDKPRNLAK SVTVE
//
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