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Database: UniProt
Entry: G9WY39_9FIRM
LinkDB: G9WY39_9FIRM
Original site: G9WY39_9FIRM 
ID   G9WY39_9FIRM            Unreviewed;       193 AA.
AC   G9WY39;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=HMPREF9629_01090 {ECO:0000313|EMBL:EHL16543.1};
OS   Peptoanaerobacter stomatis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoanaerobacter.
OX   NCBI_TaxID=796937 {ECO:0000313|EMBL:EHL16543.1, ECO:0000313|Proteomes:UP000006437};
RN   [1] {ECO:0000313|EMBL:EHL16543.1, ECO:0000313|Proteomes:UP000006437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACC19a {ECO:0000313|EMBL:EHL16543.1,
RC   ECO:0000313|Proteomes:UP000006437};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA   Epstein S., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Eubacteriaceae bacterium ACC19a.";
RL   Submitted (AUG-2011) 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};
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:EHL16543.1}.
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DR   EMBL; AFZE01000002; EHL16543.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9WY39; -.
DR   PATRIC; fig|796937.3.peg.282; -.
DR   HOGENOM; CLU_012520_6_1_9; -.
DR   BioCyc; EBAC796937-HMP:GMGH-1092-MONOMER; -.
DR   Proteomes; UP000006437; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..193
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   193 AA;  21470 MW;  4FAC053D40EAF1FD CRC64;
     MCGIVGYIGN QNAQDIVVNG LEKLEYRGYD SSGIATISNG KLELSKFKGR LSVLKEHLKK
     QPHTGFIGIG HTRWATHGEP SDVNSHPHIN ESESVAVIHN GIIENYRSLK AELIKEGYKF
     KSQTDTEVIV HLIDHYLKDS KDIMKAVNLT VKRLRGAYAL GIIYKNEPDK IIAVRNESPL
     VVGIGKGENF FCI
//
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