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Database: UniProt
Entry: A0A100IEJ1_ASPNG
LinkDB: A0A100IEJ1_ASPNG
Original site: A0A100IEJ1_ASPNG 
ID   A0A100IEJ1_ASPNG        Unreviewed;       451 AA.
AC   A0A100IEJ1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Fructose-2,6-bisphosphatase {ECO:0000313|EMBL:GAQ39780.1};
GN   ORFNames=ABL_03316 {ECO:0000313|EMBL:GAQ39780.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ39780.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ39780.1}.
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DR   EMBL; BCMY01000004; GAQ39780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IEJ1; -.
DR   PaxDb; 5061-CADANGAP00005374; -.
DR   VEuPathDB; FungiDB:An07g02100; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1087026; -.
DR   VEuPathDB; FungiDB:ATCC64974_44700; -.
DR   VEuPathDB; FungiDB:M747DRAFT_244416; -.
DR   OMA; RWIQERC; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR10606:SF44; 6-PHOSPHOFRUCTO 2-KINASE_FRUCTOSE 2,6-BISPHOSPHATASE LONG FORM; 1.
DR   PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          17..230
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   ACT_SITE        238
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        314
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         237..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   451 AA;  51319 MW;  074FD2FB59F8D5C7 CRC64;
     MSSGSIRRGN GHNYFASSDD SKICVVMVGL PARGKSLIAG KAMRYLAWVG IPARVFNVGS
     YRRAGTPQPN ANFFDPHNTE GEKMRRAAAE AAVSDMLQWF QSGKGVVAIL DATNSTKERR
     RWIHERCQEA NVETLYVESI CDDEDLIMNN ILEVKTTSPD YKGQDPEVAA LDFRNRIRNY
     EKVYETIDDN EKHFTYVKLI NVGSTVIINQ IKDYLSSRLV YYIQNLHIKP RSIWLSRHGE
     SEYNLTGKIG GDSNISERGE AYARALPGLL KKSGVPPNTK IVIWTSTLKR TIQTARHLAA
     ETGFEKLEWK ALDELDSGVC DGLTYEQIAE KYPEDFAARD EDKYNYRYRG GESYRDVVIR
     LEPIIMELER SENVIIVTHQ AVLRCIYAYF LNTPQEQSPW MEVPLHTLIK LTPRAYGTDE
     QRFKADIPAV STWRAKGTSA KHQEYPTEIK A
//
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