ID A0A3M0IQC5_HIRRU Unreviewed; 448 AA.
AC A0A3M0IQC5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN ORFNames=DUI87_33588 {ECO:0000313|EMBL:RMB90030.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB90030.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMB90030.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMB90030.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMB90030.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC {ECO:0000256|ARBA:ARBA00003771}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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:RMB90030.1}.
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DR EMBL; QRBI01000262; RMB90030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0IQC5; -.
DR STRING; 333673.A0A3M0IQC5; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
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:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
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; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR PANTHER; PTHR10606:SF15; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 1; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 11..229
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT ACT_SITE 237
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 306
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 236..243
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 448 AA; 51430 MW; 2B60747E58FBA202 CRC64;
MEEKSPKIPA SVPQFTNCPT MVILVGLPAR GKTYISKKLT RYLNWIGTPT RVFNVGEYRR
EAVPRYKNYE FFRHDNPEGV EIRRHCALTA LKDVGAYLSS EEGQVAVFDA TNTTRERRDV
ILQFAKENGY KVLFVESICD DPAIIEENIK QVKLSSPDYK GRGQDEAVAD FLKRIECYKA
TYEPLDDELD SGLSYIKIFD VGVRYLANRV QGHVQSRIVY YLMNIHVTPR AIYLSRHGES
QLNLRGRIGG DSGLSPRGQQ YAQALAQFIR SQNIRELKVW TSHMKRTIQT AEALGVPYEQ
WKALNEIDAG VCEEMTYEEI QERYPKELAL RDQDKYRYRY PKGESYEDLV QRLEPVIMEL
ERQENVLVVC HQAVMRCLLA YFLDKSAGEA LGTDELPYLK CPLHTVLKLT PVAYDFGEIP
PKPHTFTPQN VDINRTAADA LNTVPEHF
//
