ID A0A2H9L304_9ARCH Unreviewed; 241 AA.
AC A0A2H9L304;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
DE Flags: Fragment;
GN ORFNames=COU36_04100 {ECO:0000313|EMBL:PIT85313.1};
OS Candidatus Micrarchaeota archaeon CG10_big_fil_rev_8_21_14_0_10_59_7.
OC Archaea; Candidatus Micrarchaeota.
OX NCBI_TaxID=1974419 {ECO:0000313|EMBL:PIT85313.1, ECO:0000313|Proteomes:UP000228973};
RN [1] {ECO:0000313|EMBL:PIT85313.1, ECO:0000313|Proteomes:UP000228973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG10_big_fil_rev_8_21_14_0_10_59_7
RC {ECO:0000313|EMBL:PIT85313.1};
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-2017) 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:PIT85313.1}.
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; PFCC01000133; PIT85313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9L304; -.
DR Proteomes; UP000228973; 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 CDD; cd00714; GFAT; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR047084; GFAT_N.
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 ECO:0000313|EMBL:PIT85313.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIT85313.1}.
FT DOMAIN 5..222
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT NON_TER 241
FT /evidence="ECO:0000313|EMBL:PIT85313.1"
SQ SEQUENCE 241 AA; 26116 MW; 294D69B3B3D465CE CRC64;
MRFMCGIIGY VGLKSAGPIL LDGLRKLEYR GYDSVGMATF EGSGITLKKD AGGIDDVANR
ERLGEMAGSA GIGHTRWATH GGVTKENAHP HASCNGEIVV VHNGIIENFA ELRAELAERG
HSFRSQTDTE VIPHMLEEEM RRGNGIEQAV RNVVKQLHGS FALLVLCSKE PDKIVAARRE
SPLIIGLSEH GTFAASDATP FLGQTKHVAY LNDDEMAVLT QAGATYFDFN GNPIRKEVAE
I
//
