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Database: UniProt
Entry: G3BD16_CANTC
LinkDB: G3BD16_CANTC
Original site: G3BD16_CANTC 
ID   G3BD16_CANTC            Unreviewed;       557 AA.
AC   G3BD16;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase {ECO:0000313|EMBL:EGV60894.1};
GN   ORFNames=CANTEDRAFT_132536 {ECO:0000313|EMBL:EGV60894.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV60894.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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DR   EMBL; GL996528; EGV60894.1; -; Genomic_DNA.
DR   RefSeq; XP_006690108.1; XM_006690045.1.
DR   AlphaFoldDB; G3BD16; -.
DR   STRING; 590646.G3BD16; -.
DR   GeneID; 18249629; -.
DR   KEGG; cten:CANTEDRAFT_132536; -.
DR   eggNOG; KOG0234; Eukaryota.
DR   HOGENOM; CLU_006383_0_2_1; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000000707; 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:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
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   PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR   PANTHER; PTHR10606:SF39; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE YLR345W-RELATED; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EGV60894.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW   Transferase {ECO:0000313|EMBL:EGV60894.1}.
FT   DOMAIN          96..311
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          20..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  63619 MW;  90BABE6F3F996A12 CRC64;
     MTSPTSPVFA EDCELTNGFG SEPISVSTTP IPAANSGRRT TKRWSFHNDS KPNLVERPSE
     ASNQGRRRLS DITGVDGVHK EIDANHISPA QLYSTESGRL FHAGKICIVL AGLPGRGKTH
     LSVSLTRYLR WLGVKTHSFH LGDYRRRNFD DLDQSLFIED TKLRLKIINE CTNDMLNFFE
     NDKGQVAIYD AVNPFPKNRF ELHEKFKNLN IQTLFIESSV TDDTIIMKNM ESAAASSPDY
     ANWDYDKAYK DYSDRIKALM PYYIPMGDED DNNKLSYIKF INFGERIELH NSNYGYLINK
     VVFFLMNSRI KSGSVFFARC HNNSINYSDD PPLDTNGKTY AKNLCYTLIE HLQKQRKEYV
     ENIDLGIQDE DGTPGTNTPT SLKQKRSFSL DEKHLPAGAD GVDVNSMVVW TSVKKRTIES
     TKYFKAANIN VRHRIQLSQK NPGVVGSMEE DEIKEAFPTE YEQYLKDPYH HRFSRAESYH
     DLAIKIEPLI LEMERMSGDV LIIADESVLR VFYGYLMASS CFDIPYLPFS QDEIIEIKFN
     AYANVASQIP IKDFSCK
//
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