(data stored in ACNUC7421 zone)

SWISSPROT: C5BHG3_EDWI9

ID   C5BHG3_EDWI9            Unreviewed;       121 AA.
AC   C5BHG3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 44.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   OrderedLocusNames=NT01EI_0529 {ECO:0000313|EMBL:ACR67762.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67762.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-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: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-
CC       dihydropterin + glycolaldehyde. {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; CP001600; ACR67762.1; -; Genomic_DNA.
DR   RefSeq; WP_015869962.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0529; -.
DR   EnsemblBacteria; ACR67762; ACR67762; NT01EI_0529.
DR   GeneID; 7961554; -.
DR   KEGG; eic:NT01EI_0529; -.
DR   PATRIC; fig|634503.3.peg.479; -.
DR   eggNOG; ENOG4107ZVW; Bacteria.
DR   eggNOG; COG1539; LUCA.
DR   HOGENOM; HOG000217627; -.
DR   KO; K01633; -.
DR   OMA; GIYEWEK; -.
DR   OrthoDB; POG091H02IN; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0102083; F:7,8-dihydromonapterin aldolase activity; IEA:UniProtKB-EC.
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; C5BHG3.
DR   SWISS-2DPAGE; C5BHG3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079, ECO:0000313|EMBL:ACR67762.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN        4    114       FolB. {ECO:0000259|SMART:SM00905}.
SQ   SEQUENCE   121 AA;  13555 MW;  5C023729D8180A05 CRC64;
     MDIVFIEGLT VVTTIGVFEW EQTIRQRLVF DVELGWDNRR AAQSDDVAHC LSYAEVSEAI
     LQHVEPNRFA LVERVAEEVA TLLMTRFNSP WVRLRVSKPG AVAQARSVGV VIERGCRTAG
     V
//

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