Reviewed, UniProtKB/Swiss-Prot Q5WV42 (PHS_LEGPL)

Names and origin

Protein names

Recommended 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:

lpl1975

Organism

Legionella pneumophila (strain Lens) [Complete proteome] [HAMAP]

Taxonomic identifier

297245 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	113 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tetrahydrobiopterin biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	4-alpha-hydroxytetrahydrobiopterin dehydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 113	113	Putative pterin-4-alpha-carbinolamine dehydratase HAMAP MF_00434		PRO_0000231450

Sequences

	Sequence		Length	Mass (Da)
	Q5WV42-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: CFEB94D8A6D01722	FASTA	113	12,882
	10 20 30 40 50 60 MTSDLSSKHC ESCEGIGAAL NSEQIKNLLP QLNTKWEVTE DNRIIKRAFS FKNFYETMAF 70 80 90 100 110 VNAIAWIANI ENHHPDLEVG YNYCHVHFMT HALNGLTHND FICAAKIDKL LVD

References

[1]

"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity." Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C. Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR628337 Genomic DNA. Translation: CAH16215.1.
RefSeq	YP_127311.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3113926.
GenomeReviews	Gene locus lpl1975 in contig CR628337_GR.
KEGG	lpf:lpl1975.
NMPDR	fig|297245.3.peg.2422.
Organism-specific databases
LegioList	lpl1975.
CMR	Search...
Phylogenomic databases
HOGENOM	Q5WV42.
OMA	Q5WV42. ILTEWGK.
Enzyme and pathway databases
BioCyc	LPNE297245:LPL1975-MON.
Family and domain databases
HAMAP	MF_00434. [Tree]
InterPro	IPR001533. Trans/pterin_deHydtase. [Graphical view]
Gene3D	G3DSA:3.30.1360.20. Trans_pterinDh. 1 hit.
PANTHER	PTHR12599. Trans_pterinDh. 1 hit.
Pfam	PF01329. Pterin_4a. 1 hit. [Graphical view]
ProDom	PD007262. Trans_pterinDh. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

PHS_LEGPL

Accession

Primary (citable) accession number: Q5WV42

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	November 23, 2004
Last modified:	June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)