ID W7J8L8_9PSEU Unreviewed; 597 AA.
AC W7J8L8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=UO65_2356 {ECO:0000313|EMBL:EWC62369.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC62369.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC62369.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC62369.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
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:EWC62369.1}.
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DR EMBL; AYXG01000081; EWC62369.1; -; Genomic_DNA.
DR RefSeq; WP_035281569.1; NZ_AYXG01000081.1.
DR AlphaFoldDB; W7J8L8; -.
DR STRING; 909613.UO65_2356; -.
DR PATRIC; fig|909613.9.peg.2363; -.
DR eggNOG; COG0449; Bacteria.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000019277; 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:EWC62369.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EWC62369.1}.
FT DOMAIN 2..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 274..415
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 449..587
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 597 AA; 62868 MW; 25433918EBD2CCF8 CRC64;
MCGIAGITGT DDAGRALVDA LARLEYRGYD SAGIATHAPD GIEVRKSVGS VAALAALGSP
GGERRSGIAH TRWATHGAPS TRNAHPHLSH DGTTALVHNG TVRNVARLRG ELTDRGMATT
SDTDSEVLVH LIAWHRAQGV DALEAVRLTL ARVDGDYAVL VITADRPGTL IAAASGSPLL
IGTDGRAVHV ASDRAALSSG CTHCSPVLDG EVVAVTAAVP AGRTWEALTP GTTWTDKGSY
PNFLLKEINE QPQTSRAAIG ALFSPVAEGS AADWGSALDR SAVKRVCFLG CGSSYYAGQV
AASFVENLAR IPATAEPAAE FTQRDPVVEP DCLYVLISQS GETLDTLHAH RFLRRHPVQV
LSIVNVRGSS LDRESDASIP LYAGAEVSVA STKVVTNMQI AGLALASWLA RADYGSKSAA
LLELDLALPI LPTILADLLA GQDAEIRALA ESVHAFRSMY YLGRGPSWPV AREGAQKIKE
ISYIHAEAYQ ASELKHGPLA LVDPDHVSVV VAANDAGGQQ SATLIGQIQA RGGAVVVFSQ
HQDYEFDAPT VRLPAVHPLL DHIVMGVALQ VFAYHTATIL DRDVDRPRNL AKSVTVE
//
