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
//