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).
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; 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
//