(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKJ2_PSEAB

ID   A0A0H2ZKJ2_PSEAB        Unreviewed;       117 AA.
AC   A0A0H2ZKJ2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 13.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   Name=folB {ECO:0000313|EMBL:ABJ15546.1};
GN   OrderedLocusNames=PA14_07590 {ECO:0000313|EMBL:ABJ15546.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15546.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15546.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15546.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15546.1; -; Genomic_DNA.
DR   RefSeq; WP_003099587.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZKJ2; -.
DR   SMR; A0A0H2ZKJ2; -.
DR   EnsemblBacteria; ABJ15546; ABJ15546; PA14_07590.
DR   KEGG; pau:PA14_07590; -.
DR   KO; K01633; -.
DR   OMA; GIYEWEK; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000000653; 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; A0A0H2ZKJ2.
DR   SWISS-2DPAGE; A0A0H2ZKJ2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079}.
FT   DOMAIN        4    114       FolB. {ECO:0000259|SMART:SM00905}.
SQ   SEQUENCE   117 AA;  13140 MW;  5B67553C08C6B657 CRC64;
     MDRVFIEGLE VDTVIGVYDW ERGIRQCLRL DLTLGWDNRP AAAGDDLALA LDYAALSERV
     QEFARESHFQ LVETFAERLA EVLMGERGIP WLRIRVTKPG AVPAARGVGV EIERGCR
//

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