ID C6S6X8_NEIML Unreviewed; 118 AA.
AC C6S6X8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-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:CBA05791.1};
GN OrderedLocusNames=NMO_0965 {ECO:0000313|EMBL:CBA05791.1};
OS Neisseria meningitidis (strain alpha14).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=662598 {ECO:0000313|EMBL:CBA05791.1, ECO:0000313|Proteomes:UP000002054};
RN [1] {ECO:0000313|EMBL:CBA05791.1, ECO:0000313|Proteomes:UP000002054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alpha14 {ECO:0000313|Proteomes:UP000002054};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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; AM889136; CBA05791.1; -; Genomic_DNA.
DR RefSeq; WP_002221051.1; NC_013016.1.
DR AlphaFoldDB; C6S6X8; -.
DR GeneID; 83617582; -.
DR KEGG; nmi:NMO_0965; -.
DR HOGENOM; CLU_112632_0_2_4; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000002054; 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 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}.
FT DOMAIN 4..113
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 118 AA; 13381 MW; AAE9C987AEDCDCBC CRC64;
MDKIFLHGMK ADTLIGVYGW ERERLQTLIV DLDIGVPEKA GSDDDIANTV HYAEVCETLR
RHLKEQDFLL LEALAEYIAD LVLGYFGAVW VRVKIVKPGI LEGVREVGVE IERGKRED
//
