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Database: UniProt
Entry: K0UX23_MYCVA
LinkDB: K0UX23_MYCVA
Original site: K0UX23_MYCVA 
ID   K0UX23_MYCVA            Unreviewed;       581 AA.
AC   K0UX23;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=MVAC_05217 {ECO:0000313|EMBL:EJZ11682.1};
OS   Mycolicibacterium vaccae ATCC 25954.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ11682.1, ECO:0000313|Proteomes:UP000006072};
RN   [1] {ECO:0000313|EMBL:EJZ11682.1, ECO:0000313|Proteomes:UP000006072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ11682.1,
RC   ECO:0000313|Proteomes:UP000006072};
RX   PubMed=23105074; DOI=10.1128/JB.01462-12;
RA   Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA   Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT   "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL   J. Bacteriol. 194:6339-6340(2012).
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:EJZ11682.1}.
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DR   EMBL; ALQA01000007; EJZ11682.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0UX23; -.
DR   PATRIC; fig|1194972.3.peg.1057; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_7_0_11; -.
DR   Proteomes; UP000006072; Unassembled WGS sequence.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00714; GFAT; 1.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GFAT.
DR   InterPro; IPR047084; GFAT_N.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   NCBIfam; TIGR01135; glmS; 1.
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   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:EJZ11682.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJZ11682.1}.
FT   DOMAIN          1..208
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          268..410
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          441..571
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   581 AA;  61680 MW;  A0ECDA96C60783C9 CRC64;
     MDYLKVGLRR LEYRGYDSVG VAVQTADDDV VRMRTVGRID DLDRMLNQWT GARFNGAGIG
     HTRWATHGAV TPDNAHPHAD CTGQVSVVHN GIIENADLLR AELTCGGHVF ETAVDSEVLC
     HLIEDERLVE DDLVQAVQKA LARAQGSWAL AVLEKASGRI AVAAHGSPLL VARTAHGDFA
     TSDIAAVADW ADEYRILEDG DIVELSSDRW LRSGVPISAP PAHQCRWRSS DVELRDHTDF
     MAKEIDEQPE VASRLIERLR PNIADGGMWR QLGIPPFERL RVVGCGTSLN AGNVIANLVR
     SLGSLPVTTT VASEAGVEVG EPDQLSLAIS QSGETADVLR ALETPAVRDT RLLALTNNTH
     STLARVADAV VDCSAGPEIG VAATKTFICQ VISGAALMIS ALVAMDRLSV QAAGILADDL
     CRIPDRLAAA GAVARKVIPP IADELVSARG FIFIARGSGV PYAAEGALKL KELTYRWAEH
     CPAGELKHGP LALVGPGTPV IVVDNGDPKL LCNVAEVAAR GGRVITIGAR ESSVPVVDDH
     GAPWGPVAAT VPLQVLARTL ALSLGRDVDK PRNLAKSVTV E
//
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