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Q9X8I0 (FOLB_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Ordered Locus Names:SCO3400
ORF Names:SCE9.07
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length119 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin By similarity.

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.

Sequence similarities

Belongs to the DHNA family.

Ontologies

Keywords
   Biological processFolate biosynthesis
   Molecular functionLyase
   Technical termComplete 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 electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 119119Dihydroneopterin aldolase
PRO_0000168287

Sequences

Sequence LengthMass (Da)Tools
Q9X8I0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 0E865735FA1A694D

FASTA11913,002
        10         20         30         40         50         60 
MDRVALRGLK ARGHHGVFPK EREDGQTFLV DIVLGLDTRP AAADDDLAKT VHYGIVAEEV 

        70         80         90        100        110 
VAVVEGEPVN LVETLAERIA QVCLKHEGVE EVEVCVHKPD APITVPFDDV TVTIIRSRV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939116 Genomic DNA. Translation: CAB42753.1.
PIRT36326.
RefSeqNP_627606.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9X8I0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO3400.

Proteomic databases

PRIDEQ9X8I0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB42753; CAB42753; CAB42753.
GeneID1098837.
KEGGsco:SCO3400.
PATRIC23736556. VBIStrCoe124346_3463.

Phylogenomic databases

eggNOGCOG1539.
HOGENOMHOG000217628.
KOK01633.
OMATINYAEL.
OrthoDBEOG6G20SM.
PhylomeDBQ9X8I0.
ProtClustDBCLSK635777.

Enzyme and pathway databases

UniPathwayUPA00077; UER00154.

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...

Entry information

Entry nameFOLB_STRCO
AccessionPrimary (citable) accession number: Q9X8I0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 78 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

PATHWAY comments

Index of metabolic and biosynthesis pathways