ID A0A0D2ECX2_9EURO Unreviewed; 257 AA.
AC A0A0D2ECX2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=dihydroneopterin aldolase {ECO:0000256|ARBA:ARBA00013043};
DE EC=4.1.2.25 {ECO:0000256|ARBA:ARBA00013043};
DE AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|ARBA:ARBA00032903};
GN ORFNames=PV05_08812 {ECO:0000313|EMBL:KIW53223.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW53223.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW53223.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW53223.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the DHNA family.
CC {ECO:0000256|ARBA:ARBA00005708}.
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DR EMBL; KN847321; KIW53222.1; -; Genomic_DNA.
DR EMBL; KN847321; KIW53223.1; -; Genomic_DNA.
DR RefSeq; XP_013313806.1; XM_013458352.1.
DR RefSeq; XP_013313807.1; XM_013458353.1.
DR STRING; 348802.A0A0D2ECX2; -.
DR GeneID; 25330720; -.
DR HOGENOM; CLU_062068_1_0_1; -.
DR OrthoDB; 2093080at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1130.10; -; 2.
DR InterPro; IPR006156; Dihydroneopterin_aldolase.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
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; 2.
DR SMART; SM00905; FolB; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 2.
PE 3: Inferred from homology;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 130..241
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 257 AA; 28427 MW; 3BFD5F3F9645B16F CRC64;
MDKVILKNLK FDLAVGFDAW RRYGKPQPVS ITVEIHPRSN LEAAAAQDDV NLSLDYGKLY
KSISGSLTNS GAYPTIHVLI SQLAQFVPEY AFLDMDILFP KALLQVNGGV LYRLQVDNST
PGLITPNLTL DIKGIACSCI IGVNPHERLY KQSLSIDISI PVITTALGPE PTEEHYTAEL
HDMVEEVIDR VKGSSYHTIE ALASAVAQIV TMNYSHTVAK VRIEKPSAIA TIEAAAIEIT
RSKTFFENKD FWKVKRP
//