Q7ZAP3 (PHNX_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphonoacetaldehyde hydrolase
Short name=Phosphonatase
EC=3.11.1.1

Alternative name(s):
Phosphonoacetaldehyde phosphonohydrolase

Gene names

Name:	phnX
Ordered Locus Names:	STM0432

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP-Rule MF_01375
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.

Ontologies

Keywords
Ligand	Magnesium Metal-binding Schiff base
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	organic phosphonate catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphonoacetaldehyde hydrolase 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 – 269	269	Phosphonoacetaldehyde hydrolase HAMAP-Rule MF_01375		PRO_0000284601
Sites
	Active site	10	1	Nucleophile By similarity
	Active site	52	1	Schiff-base intermediate with substrate
	Metal binding	10	1	Magnesium By similarity
	Metal binding	12	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	186	1	Magnesium By similarity
Experimental info
	Mutagenesis	52	1	K → R: Complete loss of catalytic activity. Ref.1
	Sequence conflict	242 – 265	24	AHYVV…ARLAQ → RITWWIHWRIYL in AAB39641. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q7ZAP3 [UniParc]. Last modified April 17, 2007. Version 2. Checksum: 0359B0E1124A3AF3	FASTA	269	28,574
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	T46946.
RefSeq	NP_459427.1. NC_003197.1.
3D structure databases
ProteinModelPortal	Q7ZAP3.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM0432.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL19386; AAL19386; STM0432.
GeneID	1251951.
KEGG	stm:STM0432.
PATRIC	32379199. VBISalEnt20916_0461.
Phylogenomic databases
eggNOG	COG0637.
HOGENOM	HOG000217971.
KO	K05306.
OMA	EFGATWE.
ProtClustDB	PRK13478.
Enzyme and pathway databases
BioCyc	SENT99287:GCTI-433-MONOMER.
Family and domain databases
Gene3D	1.10.150.240. 1 hit. 3.40.50.1000. 2 hits.
HAMAP	MF_01375. PhnX.
InterPro	IPR023214. HAD-like_dom. IPR006402. HAD-SF_hydro_IA_v3. IPR023198. PGP_dom2. IPR006323. Phosphonoacetald_hydro. [Graphical view]
Pfam	PF13419. HAD_2. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01509. HAD-SF-IA-v3. 1 hit. TIGR01422. phosphonatase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PHNX_SALTY

Accession

Primary (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:	May 29, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program