ID A1UMW3_MYCSK Unreviewed; 298 AA.
AC A1UMW3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN OrderedLocusNames=Mkms_4982 {ECO:0000313|EMBL:ABL94171.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL94171.1};
RN [1] {ECO:0000313|EMBL:ABL94171.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL94171.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000518; ABL94171.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UMW3; -.
DR STRING; 189918.Mkms_4982; -.
DR KEGG; mkm:Mkms_4982; -.
DR HOGENOM; CLU_077077_0_0_11; -.
DR OMA; LCLVHNG; -.
DR OrthoDB; 9763290at2; -.
DR GO; GO:0016740; F:transferase 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 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:ABL94171.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABL94171.1}.
FT DOMAIN 2..298
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 298 AA; 31170 MW; 045F159B3D8240C8 CRC64;
MCGIVGLHLR NPELQPRLGE LLTGMLCEMS DRGSDSAGAA VYGDPTWTPP GHSCVSLLEI
GASPESVTDA VGSALGVPVS VTVLDATYLV TAQAESDALL AAARATFPDA LVAGFGEDLA
VLKGVGDPYT LTEAWGLSTA QGWQGVGHTR MATESAVTPS GAHPYAVGSD QCLVHNGSFA
NHATIRRELR AAGVQFDSEN DTEVGARFVA NELAAGRDVG TALKELCATF DGFYTLLVSN
RDSFAVVRDA IACKPAVIAE TSDWVAMASE YRALSGLPGV ENAAIWEPEP EVVYAWQR
//