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Database: UniProt
Entry: W6QER1_PENRF
LinkDB: W6QER1_PENRF
Original site: W6QER1_PENRF 
ID   W6QER1_PENRF            Unreviewed;       694 AA.
AC   W6QER1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-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   Name=GFA1 {ECO:0000313|EMBL:CDM34955.1};
GN   ORFNames=PROQFM164_S03g001682 {ECO:0000313|EMBL:CDM34955.1};
OS   Penicillium roqueforti (strain FM164).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34955.1};
RN   [1] {ECO:0000313|EMBL:CDM34955.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM164 {ECO:0000313|EMBL:CDM34955.1};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA   Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in cheese
RT   making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
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}.
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DR   EMBL; HG792017; CDM34955.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6QER1; -.
DR   STRING; 1365484.W6QER1; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 1705390at2759; -.
DR   UniPathway; UPA00113; UER00528.
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; 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   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:CDM34955.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDM34955.1}.
FT   DOMAIN          2..299
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          371..510
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          543..684
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   694 AA;  77357 MW;  F9AA3B544C77B9F4 CRC64;
     MCGIFGYINY LVEKDRRFII DTLLNGLSRL EYRGYDSAGL AVDGNKKNEV CAFKEVGKVA
     KLKELIDQST YDMTKTFESH AGISHTRWAT HGTPSRQNCH PHRSDPTWEF SVVHNGIITN
     YKELKALLES KGFRFETETD TECIAKLAKY LYDQHPDIEF TVLAKAVIKE LEGAFGLLLK
     SVHYPHEVIA ARKGSPLVIG VKTSKKMKVD FVDVEYSEEG VLSAEQASQN AAAKKSATSL
     LAPPDKSLLH RSQSRAFLSD DGIPQPVEFF LSSDPSAIVE HTKKVLYLED DDIAHIHEGQ
     LNIHRLTKDD GTSNVRAIQT IELELQEIMK GKFDHFMQKE IFEQPESVVN TMRGRLDVAN
     KKVTLGGLRQ YISTIRRCRR IIFIACGTSY HSCMAVRGIF EELTEIPIAV ELASDFLDRQ
     APVFRDDTCV FVSQSGETAD SLMALRYCLE RGALTVGCVN VVGSSISLLT HCGVHINAGP
     EIGVASTKAY TSQFVAMVMF ALSLSEDRAS KQDRREEIME GLGQISEQFK EILKLNDPIK
     ELCAKFFKNQ KSLLLLGRGA QFPTALEGAL KIKEISYLHC EAVMSGELKH GVLALVDENL
     PIIMILTRDR LFTKSLNAYQ QVIARGGRPI VICNEDDPEF SDALTEKINV PKTVDCLQGL
     LNVIPLQLIS YWLAVGEGLN VDFPRNLAKS VTVE
//
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