Q2S2L0 (Q2S2L0_SALRD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Putative pterin-4-alpha-carbinolamine dehydratase HAMAP MF_00434
Short name=PHS HAMAP MF_00434
EC=4.2.1.96 HAMAP MF_00434

Alternative name(s):
4-alpha-hydroxy-tetrahydropterin dehydratase HAMAP MF_00434
Pterin carbinolamine dehydratase HAMAP MF_00434

Gene names

Ordered Locus Names:

SRU_1447

Organism

Salinibacter ruber (strain DSM 13855 / M31)

Taxonomic identifier

309807 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Salinibacter

Protein attributes

Sequence length	128 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 SAAS SAAS001533
Sequence similarities	Belongs to the pterin-4-alpha-carbinolamine dehydratase family. HAMAP MF_00434

Ontologies

Keywords
Molecular function	Lyase HAMAP MF_00434 SAAS SAAS001533 EMBL ABC46318.1
Technical term	Complete proteome Reference 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...

Sequences

	Sequence		Length	Mass (Da)
	Q2S2L0 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: A3BEC880C8428745	FASTA	128	14,564
	10 20 30 40 50 60 MNRSRRSSRL RPDAPILESG FSNFLSEHQP EHMPSREPLS DDAIDDALAD LDGWSHADDK 70 80 90 100 110 120 LHKTYEFSDF REAISFVVRL SFYAEEMMHH PELENVYNTV SIALTTHDAG GKVTEMDVEL ASQIEELA

References

[1]

"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea." Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F. Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed: 16330755] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13855 / M31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000159 Genomic DNA. Translation: ABC46318.1.
RefSeq	YP_445571.1. NC_007677.1.
3D structure databases
ProteinModelPortal	Q2S2L0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2S2L0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3851239.
GenomeReviews	Gene locus SRU_1447 in contig CP000159_GR.
KEGG	sru:SRU_1447.
NMPDR	fig|309807.5.peg.1365.
PATRIC	23425325. VBISalRub86502_1502.
TIGR	SRU_1447.
Phylogenomic databases
eggNOG	COG2154.
HOGENOM	HBG705804.
OMA	DCATRID.
PhylomeDB	Q2S2L0.
ProtClustDB	CLSK2775324.
Enzyme and pathway databases
BioCyc	SRUB309807:SRU_1447-MONOMER.
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.
KO	K01724.
PANTHER	PTHR12599. Trans_pterinDh. 1 hit.
Pfam	PF01329. Pterin_4a. 1 hit. [Graphical view]
SUPFAM	SSF55248. Trans_pterinDh. 1 hit.
ProtoNet	Search...

Entry information

Entry name

Q2S2L0_SALRD

Accession

Primary (citable) accession number: Q2S2L0

Entry history

Integrated into UniProtKB/TrEMBL:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	December 14, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)