(data stored in SCRATCH zone)

SWISSPROT: A4F6S3_SACEN

ID   A4F6S3_SACEN            Unreviewed;       129 AA.
AC   A4F6S3;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   Name=folX {ECO:0000313|EMBL:CAL99747.1};
GN   OrderedLocusNames=SACE_0399 {ECO:0000313|EMBL:CAL99747.1};
GN   ORFNames=A8924_0795 {ECO:0000313|EMBL:PFG93550.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99747.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99747.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99747.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93550.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93550.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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; AM420293; CAL99747.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93550.1; -; Genomic_DNA.
DR   RefSeq; WP_009946434.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0399; -.
DR   EnsemblBacteria; CAL99747; CAL99747; SACE_0399.
DR   KEGG; sen:SACE_0399; -.
DR   eggNOG; ENOG4105KRF; Bacteria.
DR   eggNOG; COG1539; LUCA.
DR   HOGENOM; HOG000217628; -.
DR   KO; K01633; -.
DR   OMA; FYAYHGV; -.
DR   OrthoDB; 1858654at2; -.
DR   BioCyc; SERY405948:SACE_RS01960-MONOMER; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F6S3.
DR   SWISS-2DPAGE; A4F6S3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079, ECO:0000313|EMBL:CAL99747.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN        5    117       FolB. {ECO:0000259|SMART:SM00905}.
SQ   SEQUENCE   129 AA;  13737 MW;  94522D048140BB73 CRC64;
     MADRITLTGL KVRGNHGVFD HEKRDGQDFL VDITVWIDLA GAAADDDLAQ TLHYGEMAER
     AAAIVGGPSR DLIETVAAEI ADDIMTDGRA HAAEVTIHKP SAPIPLSFAD VAVTIRRSRR
     GGRGNVVPA
//

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