ID W2TW60_NECAM Unreviewed; 511 AA.
AC W2TW60;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphoglycerate mutase family protein {ECO:0000313|EMBL:ETN86300.1};
GN ORFNames=NECAME_06006 {ECO:0000313|EMBL:ETN86300.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN86300.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR EMBL; KI657580; ETN86300.1; -; Genomic_DNA.
DR RefSeq; XP_013308527.1; XM_013453073.1.
DR AlphaFoldDB; W2TW60; -.
DR STRING; 51031.W2TW60; -.
DR EnsemblMetazoa; NECAME_06006; NECAME_06006; NECAME_06006.
DR GeneID; 25346038; -.
DR KEGG; nai:NECAME_06006; -.
DR CTD; 25346038; -.
DR OMA; RCLMGYF; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000053676; 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:SF70; 6-PHOSPHOFRUCTO-2-KINASE; 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 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676}.
FT DOMAIN 47..280
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT ACT_SITE 288
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 360
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 287..294
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 511 AA; 59351 MW; 431E22A861F45DF2 CRC64;
MFFFYIGEAR KSQVFRMHDI RSAERASEIK IIFLNQVFGV CLDSSNEQVR VPNVIALVGL
PARGKTYISH KLCRYLNWIG IKTKGLFFVL SIKFFLCLSF NVGEYRRKAC KEGEFDFFSP
YNEKGTKIRD ECARLAIEDM GKYLEAKEGE VAILDATNTT RARRRLLIEY CKRSVLNPTF
RVFFIESVCD DPDIINSNIT EVKINSPDYK GIMTQEEAKE DFMKRIENYR LQYEPLDEEL
DDDLSFIKVI NAGKSFYVHN VNGHIQSRVV YFLMNIHLLP RSIYLTRHGE SEYNQIGRLG
GDSPLSENGL TYAEKLKEYF KVESLRDLRV WSSQKIRAAQ TASNMRDLAT NVEYWKVLDE
IDAGICEGLT YEDFESRYPK QFAERDKDKY HYRYPSGESY EDLVARLEPV IMELERQSDV
LVISHQAVLR CILAYFTNKN REELPYLKVP LHTVIKLTPK AYSCEVEMFK FDIEAVNTYR
EKPGHPNVGD LTPSLISQRM VSVSAPFSSY I
//
