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Protein

Dihydroneopterin aldolase

Gene

folB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 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 and dihydromonapterin at appreciable velocity.

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. dihydroneopterin aldolase activity Source: EcoCyc

GO - Biological processi

  1. folic acid biosynthetic process Source: UniProtKB-KW
  2. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

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 aldolase (EC:4.1.2.25)
Short name:
DHNA
Gene namesi
Name:folB
Synonyms:ygiG
Ordered Locus Names:b3058, JW3030
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: 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.

Expressioni

Gene expression databases

GenevestigatoriP0AC16.

Interactioni

Subunit structurei

Homooctamer.

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

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.
YP_491250.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76094; AAC76094; b3058.
BAE77109; BAE77109; BAE77109.
GeneIDi12930262.
947544.
KEGGiecj:Y75_p2984.
eco: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.
YP_491250.1. NC_007779.1.

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.
GeneIDi12930262.
947544.
KEGGiecj:Y75_p2984.
eco: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.

Gene expression databases

GenevestigatoriP0AC16.

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: CHARACTERIZATION.

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: January 7, 2015
This is version 80 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.