ID B9W8S0_CANDC Unreviewed; 1161 AA.
AC B9W8S0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=6-phosphofructo-2-kinase 1, putative {ECO:0000313|EMBL:CAX45143.1};
DE EC=2.7.1.105 {ECO:0000313|EMBL:CAX45143.1};
GN OrderedLocusNames=Cd36_08450 {ECO:0000313|CGD:CAL0000170647};
GN ORFNames=CD36_08450 {ECO:0000313|EMBL:CAX45143.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX45143.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX45143.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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DR EMBL; FM992688; CAX45143.1; -; Genomic_DNA.
DR RefSeq; XP_002417490.1; XM_002417445.1.
DR AlphaFoldDB; B9W8S0; -.
DR GeneID; 8045035; -.
DR KEGG; cdu:CD36_08450; -.
DR CGD; CAL0000170647; Cd36_08450.
DR VEuPathDB; FungiDB:CD36_08450; -.
DR eggNOG; KOG0234; Eukaryota.
DR HOGENOM; CLU_006383_3_0_1; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000002605; Chromosome 1.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:UniProtKB-EC.
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 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:SF32; 6-PHOSPHOFRUCTO-2-KINASE 1; 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 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 Kinase {ECO:0000313|EMBL:CAX45143.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000313|EMBL:CAX45143.1}.
FT DOMAIN 574..813
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..339
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1161 AA; 130365 MW; AB10429FAC81A558 CRC64;
MPPTSTDSTT NSTPSPNTNH NSPDQLHHNS QESIRNLIAA NFKQPQPSPS QQQQQCSLEP
PHSTSNLHHV SSSNSTQSSD ISPTDSGINL RQNRVKSYSI SNGALSHSRT ANKRVSFSNL
HSTNSSQLSL TSSGSSENEI YSDEDEYEAE RDNNKNTEQH HHNESSEVLL REPDFKQGKK
DVTTTTTTTQ EELLLHNSSL SSATNRSIRK KIAKFTAGSM SPSPDELSPT SSSTSLKPKK
NKSGYPNPNP YPNPYPYPSR HNFLNHYGGE KLALSKSLDS QLLEPYDSNS SVNSFLPEFN
KRPLTDTPIV STIGSPITRE QSYDDYDEDE DENEGDDDDN DDRRNINPIQ EEEGGELSTA
NKTTAATTTP LHKTKNISHL NLSELSHKDK KEGSPDAESL KHSREHAASI AAKQLVGNKQ
PQPKEEEEEE QEKFPTGTIA AQLLRKSAGI SENTGQLSYS VPSRSPPHVL IDESTPITTT
TTTSSTTVGS VVTVSSEDGK EKGKGLVMAK DVKDNLLKDL PPYMKEQFEK TPSLEKLKNL
LMHKPPPSAR KAYTLNIPGQ TSSKTSPDGK IASIDVGSKL VIVMVGLPAR GKSYITNKLT
RYLNWLQHDC RVFNVGNTRR KDKLNAGPEN QPLPDKAITP TESRSPQQHD AAFFNPDNKD
STALREKWAM DTLDQLLDYV INGSGSVGIF DATNSTKLRR KRVLKKIQQR SNGELPVLYL
ESVCNDPSII ESNIRLKLSG PDYKDMDPKL AFNDFVGRLH NYEKAYETID EEEEKIPGFQ
YVKMIDVGKK VVSFNIKGFL ASQTIYFLLN FNLCERQIWI TRHGESQDNL IGRIGGDADL
TKRGIKFAQT LTQFMNFQRQ EFRKQQLERF SSRLELKYNS LFNEDDVALL DSIPSEPNFC
VWTSMLTRAV ETGQYFNDQL YSIKELRMLN ELGGGKFEGM TYEEIQSKYP KEFASRLKNK
LSYRYPGVGG ESYLDVLTRL RPLIAEIERT TDHLLIISHR VVSRILLAYF LNLDKSVIGE
LDVPLHTLYC LESHPYGTDY TMYEYDENLD WFVKAEPEHQ KNVKEVGVVF KERKYSVVPT
APPTSKSRAV SFAVNNNTTN NKASDDVRDE IRRRLSMGTS NKPTLSVRDG DDKSITAKHL
RDLKNLRKPM GQRKTAADQL C
//
