ID D0JAX4_BLASB Unreviewed; 120 AA.
AC D0JAX4;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:ACY40312.1};
GN OrderedLocusNames=BLBBGE_292 {ECO:0000313|EMBL:ACY40312.1};
OS Blattabacterium sp. subsp. Blattella germanica (strain Bge) (Blattella
OS germanica symbiotic bacterium).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=331104 {ECO:0000313|EMBL:ACY40312.1, ECO:0000313|Proteomes:UP000002625};
RN [1] {ECO:0000313|EMBL:ACY40312.1, ECO:0000313|Proteomes:UP000002625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bge {ECO:0000313|Proteomes:UP000002625};
RX PubMed=19911043; DOI=10.1371/journal.pgen.1000721;
RA Lopez-Sanchez M.J., Neef A., Pereto J., Patino-Navarrete R., Pignatelli M.,
RA Latorre A., Moya A.;
RT "Evolutionary convergence and nitrogen metabolism in Blattabacterium strain
RT Bge, primary endosymbiont of the cockroach Blattella germanica.";
RL PLoS Genet. 5:E1000721-E1000721(2009).
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 ---------------------------------------------------------------------------
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; CP001487; ACY40312.1; -; Genomic_DNA.
DR RefSeq; WP_012840827.1; NC_013454.1.
DR AlphaFoldDB; D0JAX4; -.
DR STRING; 331104.BLBBGE_292; -.
DR KEGG; bbl:BLBBGE_292; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_1_2_10; -.
DR OrthoDB; 9803748at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000002625; Chromosome.
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|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU362079};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362079}.
FT DOMAIN 4..120
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 120 AA; 14151 MW; 431DC71A6FA6761E CRC64;
MGKIILDNIR LFGFHGCLSE EKRIGSHYTV NIEIELDFNE ASTHDNLSKT IDYVNLYYLV
KEEMKIHSKL IEHLAQRIIQ RIKKKYKEFL IEIKHIKVKI CKENPPIQGN IDRVCVILND
//
