FOLB_METEA
ID FOLB_METEA Reviewed; 130 AA.
AC P71513; C5B124;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Dihydroneopterin aldolase;
DE Short=DHNA;
DE EC=4.1.2.25;
DE AltName: Full=7,8-dihydroneopterin aldolase;
GN Name=folB; OrderedLocusNames=MexAM1_META1p1744;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9168622; DOI=10.1099/00221287-143-5-1729;
RA Chistoserdova L.V., Lidstrom M.E.;
RT "Molecular and mutational analysis of a DNA region separating two
RT methylotrophy gene clusters in Methylobacterium extorquens AM1.";
RL Microbiology 143:1729-1736(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin. {ECO:0000250|UniProtKB:P0AC16}.
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:0000250|UniProtKB:P0AC16};
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 -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
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DR EMBL; U72662; AAB58894.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS39588.1; -; Genomic_DNA.
DR RefSeq; WP_003597613.1; NC_012808.1.
DR AlphaFoldDB; P71513; -.
DR SMR; P71513; -.
DR STRING; 272630.MexAM1_META1p1744; -.
DR EnsemblBacteria; ACS39588; ACS39588; MexAM1_META1p1744.
DR KEGG; mea:Mex_1p1744; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_1_3_5; -.
DR OMA; GHYKSVA; -.
DR OrthoDB; 1858654at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
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 PANTHER; PTHR42844; PTHR42844; 1.
DR Pfam; PF02152; FolB; 1.
DR SMART; SM00905; FolB; 1.
DR TIGRFAMs; TIGR00525; folB; 1.
DR TIGRFAMs; TIGR00526; folB_dom; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis; Lyase.
FT CHAIN 1..130
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000168273"
FT ACT_SITE 100
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT CONFLICT 63
FT /note="D -> E (in Ref. 1; AAB58894)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="T -> S (in Ref. 1; AAB58894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 130 AA; 14274 MW; 36DB96E803C239CB CRC64;
MADRILVHRL AVFARHGVLP EEERLGQRFY ISLECRLDLA PAGRSDDVAA TVSYADLAEI
ALDIATNRRF ALIEALAEAI AETCLARFPR IETIAVRIDK PSAPIPAVLD YAAIEIVRGR
SDSVATTETR
