ID A0A1A8VVA2_PLAMA Unreviewed; 789 AA.
AC A0A1A8VVA2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN Name=GFPT {ECO:0000313|EMBL:SCN45027.1};
GN ORFNames=PMALA_006150 {ECO:0000313|EMBL:SBS83276.1}, PMUG01_10036400
GN {ECO:0000313|EMBL:SCN45027.1};
OS Plasmodium malariae.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5858 {ECO:0000313|EMBL:SBS83276.1, ECO:0000313|Proteomes:UP000078597};
RN [1] {ECO:0000313|Proteomes:UP000078597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SBS83276.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SCN45027.1, ECO:0000313|Proteomes:UP000219813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (JUN-2016) 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 ---------------------------------------------------------------------------
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; FLQW01000330; SBS83276.1; -; Genomic_DNA.
DR EMBL; LT594631; SCN45027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8VVA2; -.
DR VEuPathDB; PlasmoDB:PmUG01_10036400; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 1705390at2759; -.
DR Proteomes; UP000078597; Unassembled WGS sequence.
DR Proteomes; UP000219813; Chromosome 10.
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:SBS83276.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000219813};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SBS83276.1}.
FT DOMAIN 175..398
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 464..603
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 638..779
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 66..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 88076 MW; 607E5FC3548E2AD5 CRC64;
MNSKFKVLLN KLLNKIGNDC ASYKRKTSFK HFKDSLRSIV KNNSIEKRST WGVNAIYCAN
IKPITHSCSS RRSSSSSSSS SSRDSDGEMK EITNKCIMVD MRKRWKNSIL QNCVGKYGIL
NGRSLFILIA ICGLYEILNS SENKNKNRND NENEKKKKKK NVPPFGLLNK AAHCCGIMAY
VGNRDASKIL IDGIEILQNR GYDSCGISTI SNKNVLRTTK YASSSTSDAV EKLRINYMNN
HKNDSIGIAH TRWATHGSKT DENAHPHMDY DERISIVHNG IIENYRELKN FLLKNKIPFK
SNTDTEVVAN LIGYYLDQKE NFENAVVSTI KQLEGTWSFC IIHKDYPDQM ILAANGSPLH
IGFKDNEIFV ASEHSALFMF TNEYISLKDG EILSINKNNI DDLKILKKVE SIPEVIIQKT
PHPFPHWTIK EIHEQSISLS KSLNNGGRFS ILNNSVKLGG LDPYVEDLSK IENILLIGCG
TSYYAALYAK YIMNYLNCFN TVQVIDPIDF NISVIPKEKE GIIFISQSGE TRDVIKACKL
ADDLNLKKLS VINSVGSTIA NMTGRGVYVN AGREVGVAST KCFTSEVSVL TLIALWFFQN
KKNYISNNKI SSLINSLHRL PLYADTTIKS CENICKLLSY KLSNAKSILI IGNGLSYPIA
LEGALKIKEL TYIHSEGFTG SSLKHGPYAL LGGEDNIPVI MLVFNDNTKT VMINTGEQIK
SRGAHIICLT DDENLCKHFA DDIILIPNNG LLTPLLGVIP LQMMAYYTSV NKGNNPDKPR
CLAKTVTVS
//
