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P0AC16 (FOLB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroneopterin aldolase

Short name=DHNA
EC=4.1.2.25
Gene names
Name:folB
Synonyms:ygiG
Ordered Locus Names:b3058, JW3030
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length122 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin at appreciable velocity.

Catalytic activity

2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.

Subunit structure

Homooctamer.

Sequence similarities

Belongs to the DHNA family.

Sequence caution

The sequence AAA89138.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processFolate biosynthesis
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfolic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

tetrahydrofolate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiondihydroneopterin aldolase activity

Inferred from direct assay Ref.4. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 122122Dihydroneopterin aldolase
PRO_0000168269

Experimental info

Sequence conflict81 – 822EL → DV in L12966. Ref.1
Sequence conflict100 – 12223GAVAR…LKENN → ASGAGGECWRNH in L12966. Ref.1

Secondary structure

..................... 122
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AC16 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: BEA82C1E0AA38A55

FASTA12213,620
        10         20         30         40         50         60 
MDIVFIEQLS VITTIGVYDW EQTIEQKLVF DIEMAWDNRK AAKSDDVADC LSYADIAETV 

        70         80         90        100        110        120 
VSHVEGARFA LVERVAEEVA ELLLARFNSP WVRIKLSKPG AVARAANVGV IIERGNNLKE 


NN 

« Hide

References

« Hide 'large scale' references
[1]"Amplification of the bacA gene confers bacitracin resistance to Escherichia coli."
Cain B.D., Norton P.J., Eubanks W., Nick H.S., Allen C.M.
J. Bacteriol. 175:3784-3789(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / ATCC 35607 / JM83.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase."
Haussmann C., Rohdich F., Schmidt E., Bacher A., Richter G.
J. Biol. Chem. 273:17418-17424(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L12966 Genomic DNA. No translation available.
U28379 Genomic DNA. Translation: AAA89138.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76094.2.
AP009048 Genomic DNA. Translation: BAE77109.1.
PIRH65093.
RefSeqNP_417530.2. NC_000913.3.
YP_491250.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O90X-ray1.07A1-122[»]
ProteinModelPortalP0AC16.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36044N.
IntActP0AC16. 2 interactions.
STRING511145.b3058.

Proteomic databases

PaxDbP0AC16.
PRIDEP0AC16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76094; AAC76094; b3058.
BAE77109; BAE77109; BAE77109.
GeneID12930262.
947544.
KEGGecj:Y75_p2984.
eco:b3058.
PATRIC32121528. VBIEscCol129921_3151.

Organism-specific databases

EchoBASEEB1624.
EcoGeneEG11673. folB.

Phylogenomic databases

eggNOGCOG1539.
HOGENOMHOG000217627.
KOK01633.
OMAERGKIRY.
OrthoDBEOG6ND0KG.
PhylomeDBP0AC16.

Enzyme and pathway databases

BioCycEcoCyc:H2NEOPTERINALDOL-MONOMER.
ECOL316407:JW3030-MONOMER.
MetaCyc:H2NEOPTERINALDOL-MONOMER.
UniPathwayUPA00077; UER00154.

Gene expression databases

GenevestigatorP0AC16.

Family and domain databases

InterProIPR006156. Dihydroneopterin_aldolase.
IPR006157. FolB_dom.
[Graphical view]
PfamPF02152. FolB. 1 hit.
[Graphical view]
SMARTSM00905. FolB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00525. folB. 1 hit.
TIGR00526. folB_dom. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0AC16.
PROP0AC16.

Entry information

Entry nameFOLB_ECOLI
AccessionPrimary (citable) accession number: P0AC16
Secondary accession number(s): P31055, P76659, Q2M9E7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: June 11, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene