ID A0A109BIJ9_HYPSL Unreviewed; 130 AA.
AC A0A109BIJ9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=APY04_1566 {ECO:0000313|EMBL:KWT69483.1};
OS Hyphomicrobium sulfonivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT69483.1, ECO:0000313|Proteomes:UP000059074};
RN [1] {ECO:0000313|EMBL:KWT69483.1, ECO:0000313|Proteomes:UP000059074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDL6 {ECO:0000313|EMBL:KWT69483.1,
RC ECO:0000313|Proteomes:UP000059074};
RA Albers P.;
RT "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT consortium.";
RL Submitted (OCT-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}.
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:KWT69483.1}.
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DR EMBL; LMTR01000045; KWT69483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109BIJ9; -.
DR STRING; 121290.APY04_1566; -.
DR PATRIC; fig|121290.4.peg.2810; -.
DR OrthoDB; 7580479at2; -.
DR Proteomes; UP000059074; 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:KWT69483.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059074}.
FT DOMAIN 18..126
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 130 AA; 14175 MW; 01F0A980E83B8BA4 CRC64;
MSEMQNKAQG EGRILDRIFV RNLVLPIAIG VYDEEQGVTQ KVGFTIEAEV AAGVSPKGDN
IEEVPSYDDL ANAVKNIVAA GHINLVETLA ARIAERCLAD KRIVRVLVRI EKLERGPDAV
GVEIVRSRPT
//
