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Database: UniProt
Entry: H0FCA1_9BURK
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Original site: H0FCA1_9BURK 
ID   H0FCA1_9BURK            Unreviewed;       610 AA.
AC   H0FCA1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=KYC_22051 {ECO:0000313|EMBL:EHK64070.1};
OS   Achromobacter arsenitoxydans SY8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK64070.1, ECO:0000313|Proteomes:UP000003113};
RN   [1] {ECO:0000313|EMBL:EHK64070.1, ECO:0000313|Proteomes:UP000003113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8 {ECO:0000313|EMBL:EHK64070.1,
RC   ECO:0000313|Proteomes:UP000003113};
RX   PubMed=22328747; DOI=10.1128/JB.06667-11;
RA   Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT   "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT   Achromobacter arsenitoxydans SY8.";
RL   J. Bacteriol. 194:1243-1244(2012).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK64070.1}.
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DR   EMBL; AGUF01000071; EHK64070.1; -; Genomic_DNA.
DR   RefSeq; WP_008166481.1; NZ_AGUF01000071.1.
DR   AlphaFoldDB; H0FCA1; -.
DR   STRING; 477184.KYC_22051; -.
DR   PATRIC; fig|477184.5.peg.4332; -.
DR   eggNOG; COG0449; Bacteria.
DR   OrthoDB; 9761808at2; -.
DR   Proteomes; UP000003113; 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        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   DOMAIN          2..221
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          459..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;  66876 MW;  85A6E3C47FB0C7A7 CRC64;
     MCGIVGAVAQ RDITPILVEG LKRLEYRGYD SCGVAVYADG HLRRTRSTQR VAELGEQIAQ
     DKISGFTGIA HTRWATHGVP ATHNAHPHFS HLGNDEPRIA LVHNGIIENH DELRAELQAV
     GYVFESQTDT EVIAHLVNHL YAGDLFEAVQ NAVRRLHGAY AIAVFCRDEP HRVVGARQGS
     PLVVGVGQNE NFLASDALAL AGTTDQIIYL EDGDVVDLQL SRVWIVDAAG KNVEREVHTV
     HVHTGAAELG PYRHYMQKEI FEQPRAVGDT LQDIEAITPE LFGDGAYKIF KDIDSLLILA
     CGTSYYAGLT AKYWIESIAK IPVAVEIASE YRYRDSVPNP RSLVVTISQS GETADTLAAL
     KHARSLGMEH TLTICNVSTS AMVRECKLSY ITRAGVEIGV ASTKAFTTQL TALFLLTLTL
     AQVRGRLTDE QEAEHLKALR HLPAAIGSVL ALEPQIMAWA DRFASKENAL FLGRGMHYPI
     ALEGALKLKE ISYIHAEAYP AGELKHGPLA LVTEHMPVVT IAPKDELLEK LKSNMQEVRA
     RGGELYVFAD ADSKIQSAEG MHVIRMPEHY GKLSPILHTV PLQLLSYHTA CARGTDVDKP
     RNLAKSVTVE
//
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