DHNPA_PYRFU
ID DHNPA_PYRFU Reviewed; 114 AA.
AC E7FHF1;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Dihydroneopterin monophosphate aldolase;
DE Short=H2NMP aldolase;
DE EC=4.1.2.59 {ECO:0000269|PubMed:22931285};
DE AltName: Full=7,8-dihydroneopterin monophosphate aldolase;
GN OrderedLocusNames=PF1278;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=22931285; DOI=10.1021/cb300342u;
RA Crecy-Lagard V.D., Phillips G., Grochowski L.L., Yacoubi B.E., Jenney F.,
RA Adams M.W., Murzin A.G., White R.H.;
RT "Comparative genomics guided discovery of two missing archaeal enzyme
RT families involved in the biosynthesis of the pterin moiety of
RT tetrahydromethanopterin and tetrahydrofolate.";
RL ACS Chem. Biol. 7:1807-1816(2012).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin
CC monophosphate (H2NMP) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD).
CC Cannot use 7,8-dihydroneopterin (H2Neo) or 7,8-dihydroneopterin
CC triphosphate (H2NTP) as substrate. {ECO:0000269|PubMed:22931285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-phosphate = 6-hydroxymethyl-7,8-
CC dihydropterin + glycolaldehyde phosphate; Xref=Rhea:RHEA:51016,
CC ChEBI:CHEBI:44841, ChEBI:CHEBI:58762, ChEBI:CHEBI:133927;
CC EC=4.1.2.59; Evidence={ECO:0000269|PubMed:22931285};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PTPS family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81402.1; -; Genomic_DNA.
DR PIR; T44573; T44573.
DR RefSeq; WP_011012422.1; NZ_CP023154.1.
DR AlphaFoldDB; E7FHF1; -.
DR SMR; E7FHF1; -.
DR STRING; 186497.PF1278; -.
DR EnsemblBacteria; AAL81402; AAL81402; PF1278.
DR GeneID; 41713082; -.
DR KEGG; pfu:PF1278; -.
DR PATRIC; fig|186497.12.peg.1340; -.
DR eggNOG; arCOG02172; Archaea.
DR HOGENOM; CLU_111016_6_0_2; -.
DR OMA; KCEKLHG; -.
DR OrthoDB; 104644at2157; -.
DR PhylomeDB; E7FHF1; -.
DR BioCyc; MetaCyc:MON-20102; -.
DR BRENDA; 4.1.2.59; 5243.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.479.10; -; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR PANTHER; PTHR12589; PTHR12589; 1.
DR Pfam; PF01242; PTPS; 1.
DR PIRSF; PIRSF006113; PTP_synth; 1.
PE 1: Evidence at protein level;
KW Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..114
FT /note="Dihydroneopterin monophosphate aldolase"
FT /id="PRO_0000420355"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 114 AA; 13303 MW; BEBF3E4C82A1B528 CRC64;
MKARIIYRAS FDAAHAVKIE EWEELHGHTF SLEVVVEGEI KKGYVMDFLK LKKVVDGVVK
ELDHRNLNKI MDNPTTENIA LWISERIRKN LPGDVKLKRL SLWEGNEFGV ELEW
