ID A0A0N6ZVI6_9MICO Unreviewed; 129 AA.
AC A0A0N6ZVI6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN ORFNames=NI26_00725 {ECO:0000313|EMBL:AIV39158.1};
OS Curtobacterium sp. MR_MD2014.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1561023 {ECO:0000313|EMBL:AIV39158.1, ECO:0000313|Proteomes:UP000069933};
RN [1] {ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|Proteomes:UP000069933};
RA Mariita R.M., Bhatgnagar S., Hanselmann K., Hossain M.J., Dawson S.C.,
RA Korlach J., Boitano M., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K.;
RT "Isolation and characterization of species affiliated with family
RT Actinomycetaceae.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIV39158.1, ECO:0000313|Proteomes:UP000069933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR_MD2014 {ECO:0000313|EMBL:AIV39158.1,
RC ECO:0000313|Proteomes:UP000069933};
RX PubMed=26722011;
RA Mariita R.M., Bhatnagar S., Hanselmann K., Hossain M.J., Korlach J.,
RA Boitano M., Roberts R.J., Liles M.R., Moss A.G., Leadbetter J.R.,
RA Newman D.K., Dawson S.C.;
RT "Complete Genome Sequence of Curtobacterium sp. Strain MR_MD2014, Isolated
RT from Topsoil in Woods Hole, Massachusetts.";
RL Genome Announc. 3:0-0(2015).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.
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:0000256|ARBA:ARBA00001353,
CC ECO:0000256|RuleBase:RU362079};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00005013, ECO:0000256|RuleBase:RU362079}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000256|ARBA:ARBA00005708,
CC ECO:0000256|RuleBase:RU362079}.
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DR EMBL; CP009755; AIV39158.1; -; Genomic_DNA.
DR RefSeq; WP_066651406.1; NZ_CP009755.1.
DR AlphaFoldDB; A0A0N6ZVI6; -.
DR STRING; 1561023.NI26_00725; -.
DR KEGG; cum:NI26_00725; -.
DR PATRIC; fig|1561023.3.peg.145; -.
DR OrthoDB; 3212934at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000069933; Chromosome.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1130.10; -; 1.
DR InterPro; IPR006156; Dihydroneopterin_aldolase.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR NCBIfam; TIGR00525; folB; 1.
DR NCBIfam; TIGR00526; folB_dom; 1.
DR PANTHER; PTHR42844; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR PANTHER; PTHR42844:SF1; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR Pfam; PF02152; FolB; 1.
DR SMART; SM00905; FolB; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU362079};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362079};
KW Reference proteome {ECO:0000313|Proteomes:UP000069933}.
FT DOMAIN 5..117
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 129 AA; 13850 MW; 3EF92E9A74744F52 CRC64;
MRDTIRLTGV RARGNHGVFD HERADGQDFV VDVAVEVDAR VSSGSDDLAD TVHYGVVAEQ
VVAEIEGGPV DLIETLAERI ASAVLTHRAA LAVEVTVHKP QAPITVPFSD VSITIRRTRG
GSVSHEEEE
//
