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Q7ZAP3

- PHNX_SALTY

UniProt

Q7ZAP3 - PHNX_SALTY

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Protein
Phosphonoacetaldehyde hydrolase
Gene
phnX, STM0432
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in phosphonate degradation.UniRule annotation

Catalytic activityi

Phosphonoacetaldehyde + H2O = acetaldehyde + phosphate.UniRule annotation

Cofactori

Binds 1 Mg2+ ion per subunit By similarity.UniRule annotation

Kineticsi

  1. KM=40 µM for phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius)UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Nucleophile By similarity
Metal bindingi10 – 101Magnesium By similarity
Metal bindingi12 – 121Magnesium; via carbonyl oxygen By similarity
Active sitei52 – 521Schiff-base intermediate with substrate
Metal bindingi186 – 1861Magnesium By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. phosphonoacetaldehyde hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. organic phosphonate catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Schiff base

Enzyme and pathway databases

BioCyciSENT99287:GCTI-433-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphonoacetaldehyde hydrolase (EC:3.11.1.1)
Short name:
Phosphonatase
Alternative name(s):
Phosphonoacetaldehyde phosphonohydrolase
Gene namesi
Name:phnX
Ordered Locus Names:STM0432
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521K → R: Complete loss of catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Phosphonoacetaldehyde hydrolaseUniRule annotation
PRO_0000284601Add
BLAST

Expressioni

Inductioni

Induced when inorganic phosphate is limiting; this is controlled by PhoB.1 Publication

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi99287.STM0432.

Structurei

3D structure databases

ProteinModelPortaliQ7ZAP3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0637.
HOGENOMiHOG000217971.
KOiK05306.
OMAiGATWEEY.
OrthoDBiEOG6ZH2FH.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
HAMAPiMF_01375. PhnX.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
IPR006323. Phosphonoacetald_hydro.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01422. phosphonatase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7ZAP3-1 [UniParc]FASTAAdd to Basket

« Hide

MNRIHAVILD WAGTTVDFGS FAPTQIFVEA FRQAFDVEIT LAEARVPMGL    50
GKWQHIEALG KLPAVDARWQ AKFGRSMSAA DIDAIYAAFM PLQIAKVVDF 100
SSPIAGVIDT IAALRAEGIK IGSCSGYPRA VMERLVPAAA GHGYRPDHWV 150
ATDDLAAGGR PGPWMALQNV IALGIDAVAH CVKVDDAAPG ISEGLNAGMW 200
TVGLAVSGNE FGATWDAYQT MSKEDVAVRR EHAASKLYAA GAHYVVDSLA 250
DLPGVIAHIN ARLAQGERP 269
Length:269
Mass (Da):28,574
Last modified:April 17, 2007 - v2
Checksum:i0359B0E1124A3AF3
GO

Sequence cautioni

The sequence AAB39641.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAL19386.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 26524AHYVV…ARLAQ → RITWWIHWRIYL in AAB39641. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U69493 Genomic DNA. Translation: AAB39641.1. Different initiation.
AE006468 Genomic DNA. Translation: AAL19386.1. Different initiation.
PIRiT46946.
RefSeqiNP_459427.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19386; AAL19386; STM0432.
GeneIDi1251951.
KEGGistm:STM0432.
PATRICi32379199. VBISalEnt20916_0461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U69493 Genomic DNA. Translation: AAB39641.1 . Different initiation.
AE006468 Genomic DNA. Translation: AAL19386.1 . Different initiation.
PIRi T46946.
RefSeqi NP_459427.1. NC_003197.1.

3D structure databases

ProteinModelPortali Q7ZAP3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM0432.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL19386 ; AAL19386 ; STM0432 .
GeneIDi 1251951.
KEGGi stm:STM0432.
PATRICi 32379199. VBISalEnt20916_0461.

Phylogenomic databases

eggNOGi COG0637.
HOGENOMi HOG000217971.
KOi K05306.
OMAi GATWEEY.
OrthoDBi EOG6ZH2FH.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-433-MONOMER.

Family and domain databases

Gene3Di 1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
HAMAPi MF_01375. PhnX.
InterProi IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
IPR006323. Phosphonoacetald_hydro.
[Graphical view ]
Pfami PF13419. HAD_2. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01422. phosphonatase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPHNX_SALTY
AccessioniPrimary (citable) accession number: Q7ZAP3
Secondary accession number(s): P96059
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: May 14, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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