ID A0A015MZL6_RHIIW Unreviewed; 690 AA.
AC A0A015MZL6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|ARBA:ARBA00033302};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|ARBA:ARBA00029805};
GN ORFNames=RirG_071380 {ECO:0000313|EMBL:EXX72223.1};
OS Rhizophagus irregularis (strain DAOM 197198w) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1432141 {ECO:0000313|EMBL:EXX72223.1, ECO:0000313|Proteomes:UP000022910};
RN [1] {ECO:0000313|EMBL:EXX72223.1, ECO:0000313|Proteomes:UP000022910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 197198w {ECO:0000313|EMBL:EXX72223.1}, and DAOM197198w
RC {ECO:0000313|Proteomes:UP000022910};
RA Lin K., Geurts R., Zhang Z., Limpens E., Saunders D.G., Mu D., Pang E.,
RA Cao H., Cha H., Lin T., Zhou Q., Shang Y., Li Y., Ivanov S., Sharma T.,
RA Velzen R.V., Ruijter N.D., Aanen D.K., Win J., Kamoun S., Bisseling T.,
RA Huang S.;
RT "Single nucleus genome sequencing reveals high similarity among nuclei of
RT an endomycorrhizal fungus.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC supplies the amino sugars of asparagine-linked oligosaccharides of
CC glycoproteins). {ECO:0000256|ARBA:ARBA00003267}.
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 -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1. {ECO:0000256|ARBA:ARBA00004775}.
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:EXX72223.1}.
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DR EMBL; JEMT01015735; EXX72223.1; -; Genomic_DNA.
DR EMBL; JEMT01015735; EXX72224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A015MZL6; -.
DR STRING; 1432141.A0A015MZL6; -.
DR HOGENOM; CLU_012520_5_0_1; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000022910; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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 Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000022910};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..296
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 368..507
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 540..680
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 690 AA; 76645 MW; B6CC69F3A680B670 CRC64;
MCGIFAYLNY LIAKDRRTII DILTSGLSRL EYRGYDSAGL AIDGDDSGVV LIYKQVGKVA
ALKKLVAEAT VDFEKEFVSH CGMAHTRWAT HGEPSPTNSH PHRSDPKGEF TVVHNGIITN
YKELKTVLEK KGYMFESETD TEAVAKLAKY LYDTQKSNEN LSFTALVKGV IKELEGAFAL
IFKSVHFPNE IVATRRGSPL LVGVKTEKKL KVDFVDVEFG TDSAFAPTEE KVEGGLLSPT
DGHPKLRRSQ SRAFLSEDGL PQPIEYFLAS DPSAIVEHTK RVLYLEDDDI GHICDGELHI
HRLRRDDGIS AVRSIQTLEI ELAEIMKGSF DHFMQKEIYE QPESVVNTMR GRVNFESHKV
TLGGLKAYLA TIRRCRRIVF CACGTSYHSC VATRAIFEEL TEIPVSVELA SDFLDRKTPI
FRDDVCVFVS QSGETADTIL ALRYSLERGA LCLGITNTVG STISRETHCG VHINAGPEIG
VASTKAYTSQ FIALVMMAIQ LSEDRSSMTQ RRNDIIEELR KLSDHIKQVL NSDKELQQLA
KDVLYKEKSL LIMGRGFQNA TCLEGALKIK EVSYMHSEGI LAGELKHGPL ALIDENMPVI
LIMTKDSLYP KVQSALQQVT ARKGQPIIIC NDGDEGISSQ YKTIRVPQTV DCLQGLLTII
PLQLLSYHLA VLHGVDVDFP RNLAKSVTVE
//
