ID A0A0W0R5Z1_9GAMM Unreviewed; 112 AA.
AC A0A0W0R5Z1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:KTC66499.1};
GN ORFNames=Lade_1157 {ECO:0000313|EMBL:KTC66499.1}, NCTC12735_01440
GN {ECO:0000313|EMBL:VEH85804.1};
OS Legionella adelaidensis.
OG Plasmid 23 {ECO:0000313|EMBL:VEH85804.1,
OG ECO:0000313|Proteomes:UP000281170}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45056 {ECO:0000313|EMBL:KTC66499.1, ECO:0000313|Proteomes:UP000054859};
RN [1] {ECO:0000313|EMBL:KTC66499.1, ECO:0000313|Proteomes:UP000054859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1762-AUS-E {ECO:0000313|EMBL:KTC66499.1,
RC ECO:0000313|Proteomes:UP000054859};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Identification of large and diverse effector repertoires of 38 Legionella
RT species.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VEH85804.1, ECO:0000313|Proteomes:UP000281170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12735 {ECO:0000313|EMBL:VEH85804.1,
RC ECO:0000313|Proteomes:UP000281170};
RC PLASMID=23 {ECO:0000313|Proteomes:UP000281170};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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; LNKA01000001; KTC66499.1; -; Genomic_DNA.
DR EMBL; LR134432; VEH85804.1; -; Genomic_DNA.
DR RefSeq; WP_058462171.1; NZ_LR134432.1.
DR AlphaFoldDB; A0A0W0R5Z1; -.
DR STRING; 45056.Lade_1157; -.
DR KEGG; ladl:NCTC12735_01440; -.
DR PATRIC; fig|45056.6.peg.1199; -.
DR OrthoDB; 9810587at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000054859; Unassembled WGS sequence.
DR Proteomes; UP000281170; Plasmid 23.
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 Plasmid {ECO:0000313|EMBL:VEH85804.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054859}.
FT DOMAIN 4..112
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 112 AA; 12658 MW; 3D3638B7605C775D CRC64;
MDTLSVSNLA VFTFIGVYEW EQRIKQRLLL DISIPLDSSK INNNLKNTID YDALCKSVTQ
LIESNSFTLI ETVAEVVAQH IKETFHIDKL TLKVSKPEAI KNAANVSITI HR
//
