(data stored in ACNUC7421 zone)

SWISSPROT: FOLB_BACSU

ID   FOLB_BACSU              Reviewed;         120 AA.
AC   P28823;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   11-DEC-2019, entry version 116.
DE   RecName: Full=Dihydroneopterin aldolase;
DE            Short=DHNA;
DE            EC=4.1.2.25;
DE   AltName: Full=7,8-dihydroneopterin aldolase;
GN   Name=folB; Synonyms=folA, yacE; OrderedLocusNames=BSU00780;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ASB342;
RX   PubMed=2123867; DOI=10.1128/jb.172.12.7211-7226.1990;
RA   Slock J., Stahly D.P., Han C.-Y., Six E.W., Crawford I.P.;
RT   "An apparent Bacillus subtilis folic acid biosynthetic operon containing
RT   pab, an amphibolic trpG gene, a third gene required for synthesis of para-
RT   aminobenzoic acid, and the dihydropteroate synthase gene.";
RL   J. Bacteriol. 172:7211-7226(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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}.
DR   EMBL; M34053; AAA22698.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05313.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11854.1; -; Genomic_DNA.
DR   PIR; E37854; E37854.
DR   RefSeq; NP_387959.1; NC_000964.3.
DR   RefSeq; WP_003242949.1; NZ_JNCM01000028.1.
DR   SMR; P28823; -.
DR   STRING; 224308.BSU00780; -.
DR   PaxDb; P28823; -.
DR   PRIDE; P28823; -.
DR   EnsemblBacteria; CAB11854; CAB11854; BSU00780.
DR   GeneID; 937976; -.
DR   KEGG; bsu:BSU00780; -.
DR   PATRIC; fig|224308.179.peg.78; -.
DR   eggNOG; ENOG4105KRF; Bacteria.
DR   eggNOG; COG1539; LUCA.
DR   HOGENOM; HOG000217628; -.
DR   InParanoid; P28823; -.
DR   KO; K01633; -.
DR   OMA; GHYKSVA; -.
DR   PhylomeDB; P28823; -.
DR   BioCyc; BSUB:BSU00780-MONOMER; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IBA:GO_Central.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006760; P:folic acid-containing compound metabolic process; IBA:GO_Central.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00534; DHNA_DHNTPE; 1.
DR   InterPro; IPR006156; Dihydroneopterin_aldolase.
DR   InterPro; IPR006157; FolB_dom.
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;
DR   PRODOM; P28823.
DR   SWISS-2DPAGE; P28823.
KW   Folate biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..120
FT                   /note="Dihydroneopterin aldolase"
FT                   /id="PRO_0000168265"
FT   REGION          72..73
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   ACT_SITE        99
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   BINDING         21
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
FT   BINDING         53
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC16"
SQ   SEQUENCE   120 AA;  13517 MW;  39E03241DF39CBDD CRC64;
     MDKVYVEGME FYGYHGVFTE ENKLGQRFKV DLTAELDLSK AGQTDDLEQT INYAELYHVC
     KDIVEGEPVK LVETLAERIA GTVLGKFQPV QQCTVKVIKP DPPIPGHYKS VAIEITRKKS
//

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