ID A0A0F9Z671_9BACT Unreviewed; 591 AA.
AC A0A0F9Z671;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=UR30_C0012G0012 {ECO:0000313|EMBL:KKP39139.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWC2_33_13.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619061 {ECO:0000313|EMBL:KKP39139.1, ECO:0000313|Proteomes:UP000034765};
RN [1] {ECO:0000313|EMBL:KKP39139.1, ECO:0000313|Proteomes:UP000034765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKP39139.1}.
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DR EMBL; LBOR01000012; KKP39139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9Z671; -.
DR STRING; 1619061.UR30_C0012G0012; -.
DR PATRIC; fig|1619061.3.peg.1025; -.
DR Proteomes; UP000034765; 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:KKP39139.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKP39139.1}.
FT DOMAIN 2..219
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 279..418
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 445..581
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT COILED 255..282
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 591 AA; 65905 MW; 888F6C5024FA26BE CRC64;
MCGIFAYKGP QKNAAHIVIN GLKKLEYRGY DSWGIAFKNR NNEIEIHKEI GKISEIDLDS
LKDTENHLAI GHTRWATHGG VTRANAHPHS SEDKSIAVIH NGIIENYLEI KKDLQKKGHK
FASETDTEII VHLIEENMSL GFEKAFHKTL EKINGRFAII AIYDKEDKII AARKGSPLIV
GLNDEKKEYF IASDIPAFLK YTNKVMYLDD NQMVIVNDEL KFYDIQNFKS IEKRVIEIDW
HEEMAEKGDH PHFMIKEIFE QKDTLSRAIN QDEEKIKEVA QAIKSAYGTF LVGCGTAGKV
CHAASYIFSQ VAKKHVNFTF GSEFPSYHHF LTDRTLMIAV SQSGETADTL EAMEIAKEKG
VKLVSIVNVE TSTMARMSDI VLPVKAGPEK AVASTKATTS QLAILTLLAY ACADKLQEGK
QLLINTAAQI NDMINPRYEE HIETLANKIK DVESMYVIGK SLNYPMALEA AIKLQEVSYI
HAEGFAGGEL KHGPIALISE GTPCIAIIAN DETKNEILSN AMEIKARGGY IIGVSPDNNE
IFDYWLKTPD AGDASPIVNI IPIQILAYKL AVLRKNNPDM PRNLAKSVTV K
//
