ID H6RAZ0_NOCCG Unreviewed; 137 AA.
AC H6RAZ0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN Name=folB {ECO:0000313|EMBL:CCF61229.1};
GN OrderedLocusNames=NOCYR_0410 {ECO:0000313|EMBL:CCF61229.1};
OS Nocardia cyriacigeorgica (strain GUH-2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF61229.1, ECO:0000313|Proteomes:UP000008190};
RN [1] {ECO:0000313|EMBL:CCF61229.1, ECO:0000313|Proteomes:UP000008190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF61229.1,
RC ECO:0000313|Proteomes:UP000008190};
RX PubMed=22461543; DOI=10.1128/JB.00161-12;
RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA Richard Y., Cournoyer B., Blaha D.;
RT "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT cyriacigeorgica GUH-2.";
RL J. Bacteriol. 194:2098-2099(2012).
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; FO082843; CCF61229.1; -; Genomic_DNA.
DR RefSeq; WP_014348705.1; NC_016887.1.
DR AlphaFoldDB; H6RAZ0; -.
DR STRING; 1127134.NOCYR_0410; -.
DR KEGG; ncy:NOCYR_0410; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_1_1_11; -.
DR OrthoDB; 3212934at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000008190; 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 CDD; cd00534; DHNA_DHNTPE; 1.
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:UP000008190}.
FT DOMAIN 17..130
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 137 AA; 14769 MW; EA4FE5E90EFC45BE CRC64;
MNERAGRAPS RPAQDRIELR GLRVFGHHGV FDHEKHDGQE FIVDLTVQVD FTAAAASDDL
VDTVDYGALA DLAVSIVAGP PRDLIETVVS EIADAVMAAD PRIDAVEVVL HKPSAPIPHT
FADVRVVTAR QRERAAG
//
