Reviewed, UniProtKB/Swiss-Prot Q7W4J0 (PHS_BORPA)

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:

BPP3671

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	113 AA.
Sequence status	Complete.
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_0000063073

Sequences

	Sequence		Length	Mass (Da)
	Q7W4J0-1 [UniParc]. Last modified May 24, 2004. Version 2. Checksum: F8358B861AE4E932	FASTA	113	12,574
	10 20 30 40 50 60 MSTEFPMRIG AEVALPALQG WNAAAGRDAI EKRYRFDNFN AAFGFMARVA MFAEKMDHHP 70 80 90 100 110 EWRNVYNRVD VTLTTHDAGG VTELDVRMAQ FMDEAAGRLG ATGLPARADQ PRT

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640434 Genomic DNA. Translation: CAE38955.1. Different initiation.
RefSeq	NP_885828.1.
3D structure databases
SMR	Q7W4J0. Positions 11-97.
ModBase	Search...
Genome annotation databases
GeneID	1665887.
KEGG	bpa:BPP3671.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG705804.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP3671-MONOMER.
BRENDA	4.2.1.96. 263123.
Family and domain databases
HAMAP	MF_00434. Pterin_4_alpha. [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]
ProtoNet	Search...

Entry information

Entry name

PHS_BORPA

Accession

Primary (citable) accession number: Q7W4J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	February 9, 2010
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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