ID   MPTD_METKA              Reviewed;         121 AA.
AC   Q8TX89;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=MK0786;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 2-121, AND SUBUNIT.
RG   New York structural genomix research consortium (NYSGXRC);
RT   "Crystal Structure of uncharacterized conserved archaeal protein from
RT   Methanopyrus kandleri.";
RL   Submitted (FEB-2009) 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   -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC       biosynthesis. {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; AE009439; AAM02000.1; -; Genomic_DNA.
DR   PDB; 2IEC; X-ray; 2.33 A; A/B/C/D=2-121.
DR   PDBsum; 2IEC; -.
DR   AlphaFoldDB; Q8TX89; -.
DR   SMR; Q8TX89; -.
DR   STRING; 190192.MK0786; -.
DR   DNASU; 1476887; -.
DR   EnsemblBacteria; AAM02000; AAM02000; MK0786.
DR   KEGG; mka:MK0786; -.
DR   PATRIC; fig|190192.8.peg.828; -.
DR   HOGENOM; CLU_149105_1_0_2; -.
DR   OMA; FHQFVGT; -.
DR   UniPathway; UPA00065; -.
DR   EvolutionaryTrace; Q8TX89; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:2001118; P:tetrahydromethanopterin biosynthetic process; 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..121
FT                   /note="Dihydroneopterin aldolase"
FT                   /id="PRO_0000420353"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02130"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02130"
FT   HELIX           9..28
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   HELIX           38..49
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   STRAND          55..62
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   TURN            80..82
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   STRAND          83..91
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   STRAND          94..103
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   TURN            104..107
FT                   /evidence="ECO:0007829|PDB:2IEC"
FT   STRAND          108..118
FT                   /evidence="ECO:0007829|PDB:2IEC"
SQ   SEQUENCE   121 AA;  13735 MW;  944CED707FAC7743 CRC64;
     MKYFKRLSDR ERAIFEAGIT LGAIYHQFCG TPVSPGTAEE VAKCIERAAL LQPCVIDARV
     EVDVSSEDTD NYGGYTEVSG RNLRVTIVTR CGEWEAVGKL EFIEELNYPL MWVEEIRRVE
     Q