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Reviewed, UniProtKB/Swiss-Prot Q7NVH7 (PHS_CHRVO)

Last modified January 19, 2010. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative pterin-4-alpha-carbinolamine dehydratase
      Short name=PHS
    EC=4.2.1.96
Alternative name(s):
    4-alpha-hydroxy-tetrahydropterin dehydratase
    Pterin carbinolamine dehydratase
      Short name=PCD
Gene names
Ordered Locus Names: CV_2366
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(6R)-6-(L-erythro-1,2-dihydroxypropyl)-5,6,7,8-tetrahydro-4a-hydroxypterin = (6R)-6-(L-erythro-1,2-dihydroxypropyl)-7,8-dihydro-6H-pterin + H2O. HAMAP MF_00434

Sequence similarities

Belongs to the pterin-4-alpha-carbinolamine dehydratase family.

Ontologies

Keywords
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtetrahydrobiopterin biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular function4-alpha-hydroxytetrahydrobiopterin dehydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 108108Putative pterin-4-alpha-carbinolamine dehydratase HAMAP MF_00434
PRO_0000063080

Sequences

Sequence LengthMass (Da)Tools
Q7NVH7-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: FDF5BAA101C3080D

FASTA10812,240
        10         20         30         40         50         60 
MNLLELSCTP QHGQSPLADN TVKQLLSTLP DWEIVGIELR KTYRFANYHE TMAFVNALAW 

        70         80         90        100 
IANQEDHHPD MSVHYNRAVV NFSTHDAGGL TLNDFICAAK TEALFRRP 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ60038.1.
RefSeqNP_902036.1.

3D structure databases

SMRQ7NVH7. Positions 16-107.
ModBaseSearch...

Genome annotation databases

GeneID2548408.
GenomeReviewsGene locus CV_2366 in contig AE016825_GR.
KEGGcvi:CV_2366.
NMPDRfig|243365.1.peg.2366.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG705804.
OMAAKTAQLY.

Enzyme and pathway databases

BioCycCVIO243365:CV_2366-MONOMER.
BRENDA4.2.1.96. 415.

Family and domain databases

HAMAPMF_00434. Pterin_4_alpha.
[Tree]
InterProIPR001533. Trans/pterin_deHydtase.
[Graphical view]
Gene3DG3DSA:3.30.1360.20. Trans_pterinDh. 1 hit.
PANTHERPTHR12599. Trans_pterinDh. 1 hit.
PfamPF01329. Pterin_4a. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHS_CHRVO
AccessionPrimary (citable) accession number: Q7NVH7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 15, 2003
Last modified: January 19, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents