ID D4MSJ8_9FIRM Unreviewed; 149 AA.
AC D4MSJ8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN ORFNames=CL3_26900 {ECO:0000313|EMBL:CBL36734.1};
OS butyrate-producing bacterium SM4/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245012 {ECO:0000313|EMBL:CBL36734.1, ECO:0000313|Proteomes:UP000008959};
RN [1] {ECO:0000313|EMBL:CBL36734.1, ECO:0000313|Proteomes:UP000008959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM4/1 {ECO:0000313|EMBL:CBL36734.1,
RC ECO:0000313|Proteomes:UP000008959};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SM4/1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL36734.1, ECO:0000313|Proteomes:UP000008959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM4/1 {ECO:0000313|EMBL:CBL36734.1,
RC ECO:0000313|Proteomes:UP000008959};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FP929060; CBL36734.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MSJ8; -.
DR KEGG; bprm:CL3_26900; -.
DR PATRIC; fig|245012.3.peg.2069; -.
DR HOGENOM; CLU_012520_6_1_9; -.
DR BioCyc; BBAC245012:G1313-1296-MONOMER; -.
DR Proteomes; UP000008959; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00714; GFAT; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR029055; Ntn_hydrolases_N.
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 SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Isomerase {ECO:0000313|EMBL:CBL36734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008959};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBL36734.1}.
FT DOMAIN 2..149
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 149 AA; 16442 MW; E7014F7432C47A4D CRC64;
MCGIVGYIGS RPAAPILLNG LSKLEYRGYD SAGIAVYNGK QIVMEKVTGR LNRLRELTRD
GETLPGLSGI GHTRWATHGS PSDVNAHPHF NRDGSIVVVH NGIIENYVKL KQTLISRGYE
FLSETDTEVL AHLLDYYYKG KCAGNLWPP
//
