FOLB_MYCTO
ID FOLB_MYCTO Reviewed; 133 AA.
AC P9WNC4; L0TG79; O06275; P0A580;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Dihydroneopterin aldolase;
DE Short=DHNA;
DE EC=4.1.2.25 {ECO:0000250|UniProtKB:P9WNC5};
DE AltName: Full=7,8-dihydroneopterin 2'-epimerase;
DE AltName: Full=7,8-dihydroneopterin aldolase;
DE AltName: Full=7,8-dihydroneopterin epimerase;
DE EC=5.1.99.8 {ECO:0000250|UniProtKB:P9WNC5};
DE AltName: Full=7,8-dihydroneopterin hydroxylase;
DE EC=1.13.11.81 {ECO:0000250|UniProtKB:P9WNC5};
DE AltName: Full=Dihydroneopterin epimerase;
DE AltName: Full=Dihydroneopterin hydroxylase;
GN Name=folB; OrderedLocusNames=MT3712.1;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin, 7,8-dihydromonapterin and 7,8-
CC dihydroxanthopterin, respectively, in equal quantities. After longer
CC incubation times the only product is 6-hydroxymethyl-7,8-dihydropterin.
CC {ECO:0000250|UniProtKB:P9WNC5}.
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:P9WNC5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin = 7,8-dihydromonapterin;
CC Xref=Rhea:RHEA:45328, ChEBI:CHEBI:17001, ChEBI:CHEBI:71175;
CC EC=5.1.99.8; Evidence={ECO:0000250|UniProtKB:P9WNC5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate
CC + glycolaldehyde + H(+); Xref=Rhea:RHEA:45332, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17001,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:85130; EC=1.13.11.81;
CC Evidence={ECO:0000250|UniProtKB:P9WNC5};
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; AE000516; AAK48070.1; -; Genomic_DNA.
DR PIR; H70955; H70955.
DR RefSeq; WP_003419537.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNC4; -.
DR SMR; P9WNC4; -.
DR EnsemblBacteria; AAK48070; AAK48070; MT3712.1.
DR GeneID; 45427593; -.
DR KEGG; mtc:MT3712.1; -.
DR PATRIC; fig|83331.31.peg.3995; -.
DR HOGENOM; CLU_112632_1_1_11; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; Isomerase; Lyase; Oxidoreductase.
FT CHAIN 1..133
FT /note="Dihydroneopterin aldolase"
FT /id="PRO_0000427151"
FT ACT_SITE 99
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"
SQ SEQUENCE 133 AA; 14552 MW; B7BD7CD0D71AFB54 CRC64;
MADRIELRGL TVHGRHGVYD HERVAGQRFV IDVTVWIDLA EAANSDDLAD TYDYVRLASR
AAEIVAGPPR KLIETVGAEI ADHVMDDQRV HAVEVAVHKP QAPIPQTFDD VAVVIRRSRR
GGRGWVVPAG GAV
