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Database: UniProt
Entry: N1UR61_LEPIR
LinkDB: N1UR61_LEPIR
Original site: N1UR61_LEPIR 
ID   N1UR61_LEPIR            Unreviewed;        90 AA.
AC   N1UR61;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=LEP1GSC115_4982 {ECO:0000313|EMBL:EMY24355.1};
OS   Leptospira interrogans serovar Australis str. 200703203.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1085541 {ECO:0000313|EMBL:EMY24355.1, ECO:0000313|Proteomes:UP000012220};
RN   [1] {ECO:0000313|EMBL:EMY24355.1, ECO:0000313|Proteomes:UP000012220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200703203 {ECO:0000313|EMBL:EMY24355.1,
RC   ECO:0000313|Proteomes:UP000012220};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA   Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL   Submitted (FEB-2013) 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:EMY24355.1}.
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DR   EMBL; AHNY02000195; EMY24355.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1UR61; -.
DR   BioCyc; LINT1085541:G11IQ-2703-MONOMER; -.
DR   Proteomes; UP000012220; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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   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          1..90
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   90 AA;  10114 MW;  68CC4E4F98C59FA1 CRC64;
     MREFPAPGNV GIGHTRWATH GEPNQINAHP HTDTNSTVAV VHNGIIENYL ELKSQLKKKG
     HVFQSLTDTE VLPHLLEESK KTESLIKIHF
//
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