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Database: UniProt
Entry: A0A0L7R6Q7_9HYME
LinkDB: A0A0L7R6Q7_9HYME
Original site: A0A0L7R6Q7_9HYME 
ID   A0A0L7R6Q7_9HYME        Unreviewed;       530 AA.
AC   A0A0L7R6Q7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase {ECO:0000313|EMBL:KOC66560.1};
GN   ORFNames=WH47_08953 {ECO:0000313|EMBL:KOC66560.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC66560.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC66560.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC66560.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC       mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR   EMBL; KQ414646; KOC66560.1; -; Genomic_DNA.
DR   RefSeq; XP_017788994.1; XM_017933505.1.
DR   AlphaFoldDB; A0A0L7R6Q7; -.
DR   STRING; 597456.A0A0L7R6Q7; -.
DR   EnsemblMetazoa; XM_017933505.1; XP_017788994.1; LOC108571449.
DR   GeneID; 108571449; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000053825; 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   PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR   PANTHER; PTHR10606:SF65; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2, 6-BISPHOSPHATASE-LIKE PROTEIN; 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.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:KOC66560.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW   Transferase {ECO:0000313|EMBL:KOC66560.1}.
FT   DOMAIN          97..305
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          511..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        315
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        384
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         314..321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   530 AA;  59800 MW;  95B5A53F6742ADA7 CRC64;
     MPWVAACFDL LAAPILGYCL AVRKLGLQAG ILQQGGDKSV KTLADNTSDT SSLRKDKLLS
     ADTMAPSVEE QRQEHSKDKI AVRPPTIITK SPRKFAGVVI AMCGLPGRGK SQVAVCLSRR
     LNWNGDSTKV MRVSDYRRKR LEPYGEAVSH ELFRPDHTAN AALRALAQRD AMHDCAAWLA
     AGNSVAILDA TLVTRMQRAE VYDYFSGQLG YHVLFVECAC DDPLVLERNY KEILRYSADY
     IGMDPVRAEE DLRLKVAHYV RCYEPMDENT YPRIRINIAT MDIETCKVSG HVETSVLGYL
     GSVSVKPHTL YFSRHGESEF NVLGKVGGDA VLSTRGERYA QALATKFNAM RIPDLRVLTS
     RLRRTIATAR GVEAPQEHVA ALNELHAGVC EGLSYEEMQE HYPQEFAWRD QDKLRYRYPW
     GESYIDAMQR VDPVIAELQR SDNILVVSHQ AVLRCMIGFF LDKKPEELPY MEVPLHTIIR
     VTSHGYNYKL EFFKLPIECV NTTRVTVPPH FDMPDPWRNP GNGPTLVQQH
//
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