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Database: UniProt
Entry: J3JBK4_9LACO
LinkDB: J3JBK4_9LACO
Original site: J3JBK4_9LACO 
ID   J3JBK4_9LACO            Unreviewed;       119 AA.
AC   J3JBK4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   ORFNames=A11Y_118239 {ECO:0000313|EMBL:EJN55804.1};
OS   Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Loigolactobacillus.
OX   NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN55804.1, ECO:0000313|Proteomes:UP000007271};
RN   [1] {ECO:0000313|EMBL:EJN55804.1, ECO:0000313|Proteomes:UP000007271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA   Rodriguez J.M.;
RT   "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin. {ECO:0000256|ARBA:ARBA00037702,
CC       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:EJN55804.1}.
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DR   EMBL; AKFP01000032; EJN55804.1; -; Genomic_DNA.
DR   RefSeq; WP_003678614.1; NZ_AKFP01000032.1.
DR   AlphaFoldDB; J3JBK4; -.
DR   STRING; 1185325.A11Y_118239; -.
DR   GeneID; 65917530; -.
DR   PATRIC; fig|1185325.3.peg.1418; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000007271; Unassembled WGS sequence.
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   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|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007271}.
FT   DOMAIN          4..117
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   119 AA;  13687 MW;  BC8844268D839147 CRC64;
     MGLIKINNIQ VYTYNGVLPE ENRLGQRLEI DVALTVPIER LGTKDQLNET VNYAKVYDSI
     VTIAQTQQYQ LIESLANHIS QELLRQYQLV EAVQLRVRKY SVPIAGIFDN VEIEVQVKR
//
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