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Database: UniProt
Entry: D8U2I3_VOLCA
LinkDB: D8U2I3_VOLCA
Original site: D8U2I3_VOLCA 
ID   D8U2I3_VOLCA            Unreviewed;       784 AA.
AC   D8U2I3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN   ORFNames=VOLCADRAFT_105711 {ECO:0000313|EMBL:EFJ46141.1};
OS   Volvox carteri f. nagariensis.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN   [1] {ECO:0000313|EMBL:EFJ46141.1, ECO:0000313|Proteomes:UP000001058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX   PubMed=20616280; DOI=10.1126/science.1188800;
RA   Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA   Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA   Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA   Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA   Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT   "Genomic analysis of organismal complexity in the multicellular green alga
RT   Volvox carteri.";
RL   Science 329:223-226(2010).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC       {ECO:0000256|ARBA:ARBA00025673}.
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DR   EMBL; GL378353; EFJ46141.1; -; Genomic_DNA.
DR   RefSeq; XP_002952891.1; XM_002952845.1.
DR   AlphaFoldDB; D8U2I3; -.
DR   STRING; 3068.D8U2I3; -.
DR   GeneID; 9627701; -.
DR   KEGG; vcn:VOLCADRAFT_105711; -.
DR   eggNOG; KOG0234; Eukaryota.
DR   InParanoid; D8U2I3; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000001058; 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; 2.
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; 2.
DR   Pfam; PF00300; His_Phos_1; 1.
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:UP000001058}.
FT   DOMAIN          314..372
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   DOMAIN          373..431
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        447
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        536
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         446..453
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         500
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         547
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   784 AA;  80218 MW;  EEF216B8F2FB9816 CRC64;
     MLQVLSPSPL GLATPLPNPS SSTHPATTPL GCQPESQPQP ESQNSALLPS LASRSAPISA
     SNPAHSLEAQ QSTSYNQLTP GGGGGGPLHV ASSSSFHPGG GSGAAGTTRG SASVSLNGIN
     GGVSLRGNSG SSLGRSMLLF PSTAELARRL RGLVTNAAVN FRDVELMPKP QPPEGDMEGL
     MEGLMDQQGE EPDADAATGS TAASASLAAA AAEVIGRNGS GGGGGGGAAA AAAAAGGVGA
     GSDGDGSGDD GGHGAADGAA AAAAAAVAAA GGLPLPPMPL AAGVVAGVSA GCSRVRTSGA
     VVRKNKLVII MRHADQMQDA EFFDHTNEAG LEARHRALNA ALDDLTAWLR SDQGQVAVFD
     ATNTTESRRN LLAVADFLAR ISKYEEVYEP INDRNLHYIK LIDMVTGRGH MDINRISGYL
     PGKIVFFLMQ ICKAGMTSVR KIWLSRHGES EYNQKGLIGG NSSLSERGER YSRALPGALI
     ARLPQEQPVS VAVWTSTLKR TIETARFLPF PKLRWKALDE IDAGICDGMT YEQIAERYPQ
     EYEARKKDKL RYRYPSGESY MDVIQRVEPV IIELERERES VLVVAHQAVL RAVYAYFMNV
     PPEDIPRLSM PLHTLIELTP MPDGTMSEQR FPLDIDIGVG VGVGIDVEVV QEPAVGGPSA
     VGPSGPAAKG VVDGDGAARG AAECFAAAAE EVATEMAAAA AAAAAEAAGS GSPLSSVNSG
     GSCMAMMMSM QEGGGSLVLP ASPASSSPGS ATTGRDDEAV TDVVEAMGLA AGPAAAAAAV
     ATAQ
//
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