MPTD_PICTO
ID MPTD_PICTO Reviewed; 120 AA.
AC Q6L2J9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000255|HAMAP-Rule:MF_02130};
DE Short=DHNA {ECO:0000255|HAMAP-Rule:MF_02130};
DE EC=4.1.2.25 {ECO:0000255|HAMAP-Rule:MF_02130};
DE AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000255|HAMAP-Rule:MF_02130};
GN Name=mptD {ECO:0000255|HAMAP-Rule:MF_02130}; OrderedLocusNames=PTO0218;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 2-120, AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "Structure of hypothetical protein PTO0218 from Picrophilus torridus.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to
CC 6-hydroxymethyl-7,8-dihydropterin (6-HMD). {ECO:0000255|HAMAP-
CC Rule:MF_02130}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin +
CC glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02130};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_02130,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the archaeal dihydroneopterin aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_02130}.
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DR EMBL; AE017261; AAT42803.1; -; Genomic_DNA.
DR RefSeq; WP_011177019.1; NC_005877.1.
DR PDB; 2I52; X-ray; 2.08 A; A/B/C/D/E/F=2-120.
DR PDBsum; 2I52; -.
DR AlphaFoldDB; Q6L2J9; -.
DR SMR; Q6L2J9; -.
DR STRING; 263820.PTO0218; -.
DR DNASU; 2844002; -.
DR EnsemblBacteria; AAT42803; AAT42803; PTO0218.
DR GeneID; 2844002; -.
DR KEGG; pto:PTO0218; -.
DR PATRIC; fig|263820.9.peg.236; -.
DR eggNOG; arCOG04705; Archaea.
DR HOGENOM; CLU_149105_1_0_2; -.
DR OMA; FHQFVGT; -.
DR OrthoDB; 110834at2157; -.
DR EvolutionaryTrace; Q6L2J9; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1300.20; -; 1.
DR HAMAP; MF_02130; DHNA_arch; 1.
DR InterPro; IPR027508; DHN_aldolase_MptD.
DR InterPro; IPR036839; MptD_sf.
DR InterPro; IPR007181; MtpD_C.
DR Pfam; PF04038; DHNA; 1.
DR SUPFAM; SSF143560; SSF143560; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome.
FT CHAIN 1..120
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000420354"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02130"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02130"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2I52"
FT HELIX 13..32
FT /evidence="ECO:0007829|PDB:2I52"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2I52"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:2I52"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:2I52"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2I52"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:2I52"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:2I52"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:2I52"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:2I52"
SQ SEQUENCE 120 AA; 13692 MW; FE6A54DA26CF085F CRC64;
MYDPAEKYFN CTDIQRAFFE AGIKLGAIFH QYTGIPVNSE NASMAEEFIE RSTMIQPFVE
NVRISINNVK RSSGTYSYSS LNEKMLHAEV LINYNGKKVL GVLNYDEGLD YPVMYAKEVL