ID U2WDP2_9PROT Unreviewed; 146 AA.
AC U2WDP2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN ORFNames=RS24_00624 {ECO:0000313|EMBL:ERL47649.1};
OS Candidatus Micropelagos thuwalensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade; Micropelagos.
OX NCBI_TaxID=1397666 {ECO:0000313|EMBL:ERL47649.1, ECO:0000313|Proteomes:UP000016762};
RN [1] {ECO:0000313|EMBL:ERL47649.1, ECO:0000313|Proteomes:UP000016762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS24 {ECO:0000313|EMBL:ERL47649.1,
RC ECO:0000313|Proteomes:UP000016762};
RX PubMed=24785133; DOI=10.1111/1574-6941.12348;
RA Jimenez-Infante F., Ngugi D.K., Alam I., Rashid M., Baalawi W., Kamau A.A.,
RA Bajic V.B., Stingl U.;
RT "Genomic differentiation among two strains of the PS1 clade isolated from
RT geographically separated marine habitats.";
RL FEMS Microbiol. Ecol. 89:181-197(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERL47649.1}.
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DR EMBL; AWXE01000001; ERL47649.1; -; Genomic_DNA.
DR RefSeq; WP_021776666.1; NZ_AWXE01000001.1.
DR AlphaFoldDB; U2WDP2; -.
DR STRING; 1397666.RS24_00624; -.
DR eggNOG; COG1539; Bacteria.
DR OrthoDB; 7580479at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000016762; Unassembled WGS sequence.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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}; Hydrolase {ECO:0000313|EMBL:ERL47649.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362079}.
FT DOMAIN 28..142
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 146 AA; 16006 MW; 2D93AE36474CA50D CRC64;
MNKPLASKLT VTPETNVFAN APAGLMHVFV HDYKLMASIG IHPHEKINKQ NIIVSVDLSI
EDNAVSSPAD VPQQISDVVC YENITNLISD LVEHKHIDLV EQLAEEIAQL CLNLPRVTLA
RVKVAKPDAI ETAGSVGVTI ERFKTF
//
