(data stored in ACNUC7421 zone)

SWISSPROT: D6XV66_BACIE

ID   D6XV66_BACIE            Unreviewed;       124 AA.
AC   D6XV66;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   OrderedLocusNames=Bsel_0074 {ECO:0000313|EMBL:ADH97624.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97624.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97624.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362079};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
CC       amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
CC       from 7,8-dihydroneopterin triphosphate: step 3/4.
CC       {ECO:0000256|RuleBase:RU362079}.
CC   -!- SIMILARITY: Belongs to the DHNA family.
CC       {ECO:0000256|RuleBase:RU362079}.
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DR   EMBL; CP001791; ADH97624.1; -; Genomic_DNA.
DR   RefSeq; WP_013171054.1; NC_014219.1.
DR   STRING; 439292.Bsel_0074; -.
DR   EnsemblBacteria; ADH97624; ADH97624; Bsel_0074.
DR   KEGG; bse:Bsel_0074; -.
DR   eggNOG; ENOG4105KRF; Bacteria.
DR   eggNOG; COG1539; LUCA.
DR   HOGENOM; HOG000217628; -.
DR   KO; K01633; -.
DR   OMA; FYAYHGV; -.
DR   OrthoDB; 1858654at2; -.
DR   BioCyc; BSEL439292:G1GLR-81-MONOMER; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000000271; 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   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; D6XV66.
DR   SWISS-2DPAGE; D6XV66.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079, ECO:0000313|EMBL:ADH97624.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN        4    117       FolB. {ECO:0000259|SMART:SM00905}.
SQ   SEQUENCE   124 AA;  14063 MW;  40A2B98FAF8588BE CRC64;
     MDKVFVEGMK FYGYHGAYRA ENELGQRFEA DVLMEMDSKK AAETDALEDT VNYALVYETV
     RDIIEGEAVN LVETLANRVA DDILRKFHLV EACTVKVTKP DPPIPGHYDA VAVQVRRSRD
     HHAH
//

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