MPTD_METJA
ID MPTD_METJA Reviewed; 121 AA.
AC Q57851;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Dihydroneopterin aldolase {ECO:0000255|HAMAP-Rule:MF_02130, ECO:0000303|PubMed:24982305};
DE Short=DHNA {ECO:0000255|HAMAP-Rule:MF_02130, ECO:0000303|PubMed:22931285};
DE EC=4.1.2.25 {ECO:0000255|HAMAP-Rule:MF_02130, ECO:0000269|PubMed:22931285, ECO:0000269|PubMed:24982305};
DE AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000255|HAMAP-Rule:MF_02130, ECO:0000303|PubMed:22931285};
GN Name=mptD {ECO:0000255|HAMAP-Rule:MF_02130}; OrderedLocusNames=MJ0408;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND PATHWAY.
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).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP GLU-25; HIS-35; GLN-61; TYR-78 AND TYR-111.
RX PubMed=24982305; DOI=10.1128/jb.01812-14;
RA Wang Y., Xu H., Grochowski L.L., White R.H.;
RT "Biochemical characterization of a dihydroneopterin aldolase used for
RT methanopterin biosynthesis in methanogens.";
RL J. Bacteriol. 196:3191-3198(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 2-121 IN COMPLEX WITH PTERIN
RP ANALOG, AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of hypothetical protein MJ0408 from Methanococcus
RT jannaschii.";
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, ECO:0000269|PubMed:22931285}.
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 ECO:0000269|PubMed:22931285, ECO:0000269|PubMed:24982305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=64.5 uM for 7,8-dihydroneopterin (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:24982305};
CC KM=9.9 uM for 7,8-dihydroneopterin (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:24982305};
CC Note=kcat is 0.07 sec(-1) at 25 degrees Celsius. kcat is 1.0 sec(-1)
CC at 70 degrees Celsius. {ECO:0000269|PubMed:24982305};
CC pH dependence:
CC Optimum pH is 8.3. {ECO:0000269|PubMed:24982305};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02130,
CC ECO:0000269|PubMed:22931285}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_02130,
CC ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the archaeal dihydroneopterin aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_02130}.
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DR EMBL; L77117; AAB98398.1; -; Genomic_DNA.
DR PIR; H64350; H64350.
DR RefSeq; WP_010869907.1; NC_000909.1.
DR PDB; 2OGF; X-ray; 1.89 A; A/B/C/D=2-121.
DR PDBsum; 2OGF; -.
DR AlphaFoldDB; Q57851; -.
DR SMR; Q57851; -.
DR STRING; 243232.MJ_0408; -.
DR EnsemblBacteria; AAB98398; AAB98398; MJ_0408.
DR GeneID; 1451268; -.
DR KEGG; mja:MJ_0408; -.
DR eggNOG; arCOG04705; Archaea.
DR HOGENOM; CLU_149105_1_0_2; -.
DR InParanoid; Q57851; -.
DR OMA; FHQFVGT; -.
DR OrthoDB; 110834at2157; -.
DR PhylomeDB; Q57851; -.
DR BioCyc; MetaCyc:MON-17933; -.
DR UniPathway; UPA00065; -.
DR EvolutionaryTrace; Q57851; -.
DR Proteomes; UP000000805; 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_0000106857"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.4"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.4"
FT MUTAGEN 25
FT /note="E->Q: Has 25-fold higher Km towards 7,8-
FT dihydroneopterin than wild-type."
FT /evidence="ECO:0000269|PubMed:24982305"
FT MUTAGEN 35
FT /note="H->N: Has 20-fold lower kcat than wild-type."
FT /evidence="ECO:0000269|PubMed:24982305"
FT MUTAGEN 61
FT /note="Q->A: Has 20-fold lower kcat than wild-type."
FT /evidence="ECO:0000269|PubMed:24982305"
FT MUTAGEN 78
FT /note="Y->F: Has 20-fold lower kcat than wild-type."
FT /evidence="ECO:0000269|PubMed:24982305"
FT MUTAGEN 111
FT /note="Y->F: Has 2-fold lower kcat than wild-type."
FT /evidence="ECO:0000269|PubMed:24982305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2OGF"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:2OGF"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:2OGF"
FT HELIX 18..37
FT /evidence="ECO:0007829|PDB:2OGF"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2OGF"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2OGF"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:2OGF"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2OGF"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:2OGF"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:2OGF"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2OGF"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:2OGF"
SQ SEQUENCE 121 AA; 14182 MW; 281669A0B3616F73 CRC64;
MRVEETEVFK KYFKNLTDRE RAVFEGGITL GALFHQFVGT PVSKYNKESL ERAIEEAMKN
QPCVYDIKVK IRNVGEKYVS LDGKMLDVDL KIKINKTVAH LKLEYIPEID YPLMYVKKFE
E
