ID A0A011MFB3_9PROT Unreviewed; 118 AA.
AC A0A011MFB3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=folB {ECO:0000313|EMBL:EXI68463.1};
GN ORFNames=AW08_01245 {ECO:0000313|EMBL:EXI68463.1};
OS Candidatus Accumulibacter adjunctus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI68463.1, ECO:0000313|Proteomes:UP000020218};
RN [1] {ECO:0000313|EMBL:EXI68463.1, ECO:0000313|Proteomes:UP000020218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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}.
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:EXI68463.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JFAX01000005; EXI68463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011MFB3; -.
DR STRING; 1454001.AW08_01245; -.
DR PATRIC; fig|1454001.3.peg.1269; -.
DR Proteomes; UP000020218; Unassembled WGS sequence.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006760; P:folic acid-containing compound metabolic process; IEA:InterPro.
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; 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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EXI68463.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020218}.
FT DOMAIN 4..114
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 118 AA; 12834 MW; EC097F9302B362E7 CRC64;
MDIIFIDELR ATTLIGIYPR EQAMPQTVEI SLQIGTSTAS AGASDDIGDT IDYARVVERL
RAELAARHFN LLERLAEYVA ALLLEDFGAT WVRVSIAKLG MMRGVARVGV VIERGAAA
//
