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
//