Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 to dihydromonapterin at appreciable velocity.1 Publication

Catalytic activityi

7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.1 Publication
7,8-dihydroneopterin = 7,8-dihydromonapterin.1 Publication

Kineticsi

  1. KM=64 µM for 7,8-dihydroneopterin in aldolase reaction1 Publication
  2. KM=45 µM for 7,8-dihydroneopterin in epimerase reaction1 Publication
  3. KM=36 µM for 7,8-dihydromonapterin in aldolase reaction1 Publication
  4. KM=57 µM for 7,8-dihydromonapterin in epimerase reaction1 Publication
  1. Vmax=127 µmol/h/mg enzyme toward 7,8-dihydroneopterin in aldolase reaction1 Publication
  2. Vmax=20.3 µmol/h/mg enzyme toward 7,8-dihydroneopterin in epimerase reaction1 Publication
  3. Vmax=158 µmol/h/mg enzyme toward 7,8-dihydromonapterin in aldolase reaction1 Publication
  4. Vmax=15.6 µmol/h/mg enzyme toward 7,8-dihydromonapterin in epimerase reaction1 Publication

Pathway:itetrahydrofolate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Dihydroneopterin aldolase (folB)
  4. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (folK)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211SubstrateCombined sources1 Publication
Binding sitei53 – 531SubstrateCombined sources1 Publication
Active sitei98 – 981Proton donor/acceptorBy similarity1 Publication

GO - Molecular functioni

  • dihydroneopterin aldolase activity Source: EcoCyc
  • isomerase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Folate biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:H2NEOPTERINALDOL-MONOMER.
ECOL316407:JW3030-MONOMER.
MetaCyc:H2NEOPTERINALDOL-MONOMER.
UniPathwayiUPA00077; UER00154.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroneopterin aldolase1 Publication (EC:4.1.2.251 Publication)
Short name:
DHNA1 Publication
Alternative name(s):
7,8-dihydroneopterin 2'-epimerase
7,8-dihydroneopterin aldolase
7,8-dihydroneopterin epimerase (EC:5.1.99.-1 Publication)
Dihydroneopterin epimerase
Gene namesi
Name:folB1 Publication
Synonyms:ygiG
Ordered Locus Names:b3058, JW3030
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11673. folB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122Dihydroneopterin aldolasePRO_0000168269Add
BLAST

Proteomic databases

PaxDbiP0AC16.
PRIDEiP0AC16.

Interactioni

Subunit structurei

Homooctamer.1 Publication

Protein-protein interaction databases

DIPiDIP-36044N.
IntActiP0AC16. 2 interactions.
STRINGi511145.b3058.

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1514Combined sources
Helixi19 – 235Combined sources
Beta strandi26 – 3611Combined sources
Helixi39 – 446Combined sources
Helixi47 – 493Combined sources
Helixi53 – 6412Combined sources
Beta strandi68 – 703Combined sources
Helixi72 – 8615Combined sources
Beta strandi92 – 976Combined sources
Beta strandi109 – 1146Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O90X-ray1.07A1-122[»]
ProteinModelPortaliP0AC16.
SMRiP0AC16. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC16.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 732Substrate bindingCombined sources1 Publication

Sequence similaritiesi

Belongs to the DHNA family.Curated

Phylogenomic databases

eggNOGiCOG1539.
HOGENOMiHOG000217627.
InParanoidiP0AC16.
KOiK01633.
OMAiGIYEWEK.
OrthoDBiEOG6ND0KG.
PhylomeDBiP0AC16.

Family and domain databases

InterProiIPR006156. Dihydroneopterin_aldolase.
IPR006157. FolB_dom.
[Graphical view]
PfamiPF02152. FolB. 1 hit.
[Graphical view]
SMARTiSM00905. FolB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00525. folB. 1 hit.
TIGR00526. folB_dom. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AC16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIVFIEQLS VITTIGVYDW EQTIEQKLVF DIEMAWDNRK AAKSDDVADC
60 70 80 90 100
LSYADIAETV VSHVEGARFA LVERVAEEVA ELLLARFNSP WVRIKLSKPG
110 120
AVARAANVGV IIERGNNLKE NN
Length:122
Mass (Da):13,620
Last modified:November 8, 2005 - v1
Checksum:iBEA82C1E0AA38A55
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 822EL → DV in L12966 (PubMed:8389741).Curated
Sequence conflicti100 – 12223GAVAR…LKENN → ASGAGGECWRNH in L12966 (PubMed:8389741).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH65093.
RefSeqiNP_417530.2. NC_000913.3.
WP_001295541.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76094; AAC76094; b3058.
BAE77109; BAE77109; BAE77109.
GeneIDi947544.
KEGGieco:b3058.
PATRICi32121528. VBIEscCol129921_3151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH65093.
RefSeqiNP_417530.2. NC_000913.3.
WP_001295541.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O90X-ray1.07A1-122[»]
ProteinModelPortaliP0AC16.
SMRiP0AC16. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36044N.
IntActiP0AC16. 2 interactions.
STRINGi511145.b3058.

Proteomic databases

PaxDbiP0AC16.
PRIDEiP0AC16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76094; AAC76094; b3058.
BAE77109; BAE77109; BAE77109.
GeneIDi947544.
KEGGieco:b3058.
PATRICi32121528. VBIEscCol129921_3151.

Organism-specific databases

EchoBASEiEB1624.
EcoGeneiEG11673. folB.

Phylogenomic databases

eggNOGiCOG1539.
HOGENOMiHOG000217627.
InParanoidiP0AC16.
KOiK01633.
OMAiGIYEWEK.
OrthoDBiEOG6ND0KG.
PhylomeDBiP0AC16.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00154.
BioCyciEcoCyc:H2NEOPTERINALDOL-MONOMER.
ECOL316407:JW3030-MONOMER.
MetaCyc:H2NEOPTERINALDOL-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AC16.
PROiP0AC16.

Family and domain databases

InterProiIPR006156. Dihydroneopterin_aldolase.
IPR006157. FolB_dom.
[Graphical view]
PfamiPF02152. FolB. 1 hit.
[Graphical view]
SMARTiSM00905. FolB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00525. folB. 1 hit.
TIGR00526. folB_dom. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
  5. "Crystallographic and molecular dynamics simulation analysis of Escherichia coli dihydroneopterin aldolase."
    Blaszczyk J., Lu Z., Li Y., Yan H., Ji X.
    Cell Biosci. 4:52-52(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEX WITH L-NEOPTERIN, REACTION MECHANISM.

Entry informationi

Entry nameiFOLB_ECOLI
AccessioniPrimary (citable) accession number: P0AC16
Secondary accession number(s): P31055, P76659, Q2M9E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: July 22, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.