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Database: UniProt
Entry: A5EWI1_DICNV
LinkDB: A5EWI1_DICNV
Original site: A5EWI1_DICNV 
ID   A5EWI1_DICNV            Unreviewed;       265 AA.
AC   A5EWI1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   Name=vrlG {ECO:0000313|EMBL:ABQ13403.1};
GN   OrderedLocusNames=DNO_0185 {ECO:0000313|EMBL:ABQ13403.1};
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195 {ECO:0000313|EMBL:ABQ13403.1, ECO:0000313|Proteomes:UP000000248};
RN   [1] {ECO:0000313|EMBL:ABQ13403.1, ECO:0000313|Proteomes:UP000000248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A {ECO:0000313|EMBL:ABQ13403.1,
RC   ECO:0000313|Proteomes:UP000000248};
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
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; CP000513; ABQ13403.1; -; Genomic_DNA.
DR   RefSeq; WP_011927935.1; NC_009446.1.
DR   AlphaFoldDB; A5EWI1; -.
DR   STRING; 246195.DNO_0185; -.
DR   KEGG; dno:DNO_0185; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_1049414_0_0_6; -.
DR   OMA; LTIRHED; -.
DR   OrthoDB; 3456346at2; -.
DR   Proteomes; UP000000248; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00352; Gn_AT_II; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, 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   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000313|EMBL:ABQ13403.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000248};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABQ13403.1}.
FT   DOMAIN          2..238
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   265 AA;  30431 MW;  1099A45E063852B2 CRC64;
     MCGQVGIIFG RKRRRPDERD YLCELFIRML LHSEERGPHA SGLAWLKTDG SHRIFKRPMR
     AHELVYEKPF QELLGQVDNE TTVLMGHTRW RTRGNEFNNR NNHPIRAGIV IGTHNGTIYN
     ADYLFRRLGL PRYAEVESEL IFRLADRFAP EGPIDQEDLK KALALCRGQM SAVLASRLDP
     GTITVLKGNK PLCLCIHRQH RVVLYASEAA FIDFAVDSES GWRELEVPPM TMLTIRHEDV
     RAIENSEFRF IPQERKGTIP EGVNA
//
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