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Database: UniProt
Entry: A0A250XI35_9CHLO
LinkDB: A0A250XI35_9CHLO
Original site: A0A250XI35_9CHLO 
ID   A0A250XI35_9CHLO        Unreviewed;       561 AA.
AC   A0A250XI35;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN   ORFNames=CEUSTIGMA_g10167.t1 {ECO:0000313|EMBL:GAX82741.1};
OS   Chlamydomonas eustigma.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX82741.1, ECO:0000313|Proteomes:UP000232323};
RN   [1] {ECO:0000313|EMBL:GAX82741.1, ECO:0000313|Proteomes:UP000232323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX82741.1,
RC   ECO:0000313|Proteomes:UP000232323};
RA   Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA   Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT   "Acidophilic green algal genome provides insights into adaptation to an
RT   acidic environment.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:GAX82741.1}.
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DR   EMBL; BEGY01000085; GAX82741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A250XI35; -.
DR   STRING; 1157962.A0A250XI35; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000232323; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232323}.
FT   DOMAIN          119..334
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         349..356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         403
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   561 AA;  62472 MW;  0AFF73343CE01B0B CRC64;
     MWDHVTRAKD SEKSIESTPR STSAGGHATP SFSAFNAVIK SSFSGTSSAE VSPSKPNLEK
     ILRQPVNFRD VVITTTQSSI SGGLNSPTKS VEIDLHASTS VGNLAEVDSL GSLYSEQPQY
     ASVQRSKMVI IMVGLPGRGK TFVCNKLKCY LNWLGHVTGH FNVGNYRRNQ KLGDLTQDAS
     FFCHTNGAGL ELRQKALDSA LDDMMRWLNT GSGQVAIFDA TNTTASRRQL LRDKLHGRCQ
     YLFIESICND METLERNYMN KLMYSPDYAG VNVEEALRDF KARIQAYEDV YEPITDRSFH
     YIKLIDMVTG RGYMDINRIS GYIPGKLVFF LMQVCRAGLG NARKIWLTRH GESEYNVLKL
     IGGDSNISGE GEKYATALPK VLEARLPQGE ATPLQVWTST LKRTIQTAQH LPFAKLRWKA
     LDEIDAGVCD GMTYEDIAEK MPEEFAARKS DKLGYRYPSG ESYMDVIQRL EPVIIEIERQ
     KDSVCIVAHQ AILRVIYGYF MAVSPEEIPR LSIPLHTLIE LTPMPDGQMS VQMLPVDINA
     DPSTLLENLA SNPSPLPVLA S
//
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