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Q7ZAP3 (PHNX_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Phosphonoacetaldehyde hydrolase

Short name=Phosphonatase
EC=3.11.1.1
Alternative name(s):
Phosphonoacetaldehyde phosphonohydrolase
Gene names
Name:phnX
Ordered Locus Names:STM0432
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in phosphonate degradation. HAMAP-Rule MF_01375

Catalytic activity

Phosphonoacetaldehyde + H2O = acetaldehyde + phosphate. HAMAP-Rule MF_01375

Cofactor

Binds 1 Mg2+ ion per subunit By similarity. HAMAP-Rule MF_01375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01375

Induction

Induced when inorganic phosphate is limiting; this is controlled by PhoB. Ref.3

Miscellaneous

Maps to a phosphate-starvation-inducible locus previously known as psiC.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. PhnX family.

Biophysicochemical properties

Kinetic parameters:

KM=40 µM for phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius) HAMAP-Rule MF_01375

Sequence caution

The sequence AAB39641.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAL19386.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 269269Phosphonoacetaldehyde hydrolase HAMAP-Rule MF_01375
PRO_0000284601

Sites

Active site101Nucleophile By similarity
Active site521Schiff-base intermediate with substrate
Metal binding101Magnesium By similarity
Metal binding121Magnesium; via carbonyl oxygen By similarity
Metal binding1861Magnesium By similarity

Experimental info

Mutagenesis521K → R: Complete loss of catalytic activity. Ref.1
Sequence conflict242 – 26524AHYVV…ARLAQ → RITWWIHWRIYL in AAB39641. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7ZAP3 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 0359B0E1124A3AF3

FASTA26928,574
        10         20         30         40         50         60 
MNRIHAVILD WAGTTVDFGS FAPTQIFVEA FRQAFDVEIT LAEARVPMGL GKWQHIEALG 

        70         80         90        100        110        120 
KLPAVDARWQ AKFGRSMSAA DIDAIYAAFM PLQIAKVVDF SSPIAGVIDT IAALRAEGIK 

       130        140        150        160        170        180 
IGSCSGYPRA VMERLVPAAA GHGYRPDHWV ATDDLAAGGR PGPWMALQNV IALGIDAVAH 

       190        200        210        220        230        240 
CVKVDDAAPG ISEGLNAGMW TVGLAVSGNE FGATWDAYQT MSKEDVAVRR EHAASKLYAA 

       250        260 
GAHYVVDSLA DLPGVIAHIN ARLAQGERP 

« Hide

References

« Hide 'large scale' references
[1]"Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis."
Baker A.S., Ciocci M.J., Metcalf W.W., Kim J., Babbitt P.C., Wanner B.L., Martin B.M., Dunaway-Mariano D.
Biochemistry 37:9305-9315(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, BIOPHYSICAL CHARACTERIZATION, REACTION MECHANISM, SCHIFF BASE, MUTAGENESIS OF LYS-52.
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Molecular cloning, mapping, and regulation of Pho regulon genes for phosphonate breakdown by the phosphonatase pathway of Salmonella typhimurium LT2."
Jiang W., Metcalf W.W., Lee K.-S., Wanner B.L.
J. Bacteriol. 177:6411-6421(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, CLONING, INDUCTION.
Strain: LT2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U69493 Genomic DNA. Translation: AAB39641.1. Different initiation.
AE006468 Genomic DNA. Translation: AAL19386.1. Different initiation.
PIRT46946.
RefSeqNP_459427.1. NC_003197.1.

3D structure databases

ProteinModelPortalQ7ZAP3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM0432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19386; AAL19386; STM0432.
GeneID1251951.
KEGGstm:STM0432.
PATRIC32379199. VBISalEnt20916_0461.

Phylogenomic databases

eggNOGCOG0637.
HOGENOMHOG000217971.
KOK05306.
OMAFDWAGTM.
OrthoDBEOG6ZH2FH.
ProtClustDBPRK13478.

Enzyme and pathway databases

BioCycSENT99287:GCTI-433-MONOMER.

Family and domain databases

Gene3D1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
HAMAPMF_01375. PhnX.
InterProIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
IPR006323. Phosphonoacetald_hydro.
[Graphical view]
PfamPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01422. phosphonatase. 1 hit.
ProtoNetSearch...

Entry information

Entry namePHNX_SALTY
AccessionPrimary (citable) accession number: Q7ZAP3
Secondary accession number(s): P96059
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 73 of the entry and version 2 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