P16679 (PHNL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL
Short name=RPnTP synthase subunit PhnL
EC=2.7.8.37

Gene names

Name:	phnL
Ordered Locus Names:	b4096, JW4057

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Together with PhnG, PhnH and PhnI is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. Ref.6
Catalytic activity	ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine. Ref.6
Sequence similarities	Belongs to the ABC transporter superfamily. Contains 1 ABC transporter domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC organic phosphonate catabolic process Inferred from mutant phenotype PubMed 8388873. Source: EcoCyc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 226	226	Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL		PRO_0000092745
Regions
	Domain	2 – 226	225	ABC transporter
	Nucleotide binding	41 – 48	8	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	P16679 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 195EC8BB5A2D21D2	FASTA	226	24,705
	10 20 30 40 50 60 MINVQNVSKT FILHQQNGVR LPVLNRASLT VNAGECVVLH GHSGSGKSTL LRSLYANYLP 70 80 90 100 110 120 DEGQIQIKHG DEWVDLVTAP ARKVVEIRKT TVGWVSQFLR VIPRISALEV VMQPLLDTGV 130 140 150 160 170 180 PREACAAKAA RLLTRLNVPE RLWHLAPSTF SGGEQQRVNI ARGFIVDYPI LLLDEPTASL 190 200 210 220 DAKNSAAVVE LIREAKTRGA AIVGIFHDEA VRNDVADRLH PMGASS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B." Chen C.-M., Ye Q.-Z., Zhu Z., Wanner B.L., Walsh C.T. J. Biol. Chem. 265:4461-4471(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B.
[2]	"Molecular analysis of the cryptic and functional phn operons for phosphonate use in Escherichia coli K-12." Makino K., Kim S.K., Shinagawa H., Amemura M., Nakata A. J. Bacteriol. 173:2665-2672(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Intermediates in the transformation of phosphonates to phosphate by bacteria." Kamat S.S., Williams H.J., Raushel F.M. Nature 480:570-573(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY. Strain: K12.
[7]	"Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway." Jochimsen B., Lolle S., McSorley F.R., Nabi M., Stougaard J., Zechel D.L., Hove-Jensen B. Proc. Natl. Acad. Sci. U.S.A. 108:11393-11398(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05260 Genomic DNA. Translation: AAA24350.1. D90227 Genomic DNA. Translation: BAA14272.1. U14003 Genomic DNA. Translation: AAA96995.1. U00096 Genomic DNA. Translation: AAC77057.1. AP009048 Genomic DNA. Translation: BAE78099.1.
PIR	D35719.
RefSeq	NP_418520.1. NC_000913.2. YP_492240.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P16679.
SMR	P16679. Positions 23-208.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16679. 3 interactions.
STRING	511145.b4096.
Proteomic databases
PaxDb	P16679.
PRIDE	P16679.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC77057; AAC77057; b4096. BAE78099; BAE78099; BAE78099.
GeneID	12933025. 948612.
KEGG	ecj:Y75_p3984. eco:b4096.
PATRIC	32123751. VBIEscCol129921_4224.
Organism-specific databases
EchoBASE	EB0715.
EcoGene	EG10721. phnL.
Phylogenomic databases
eggNOG	COG4778.
KO	K05780.
OMA	NVSKTFV.
ProtClustDB	CLSK880846.
Enzyme and pathway databases
BioCyc	EcoCyc:PHNL-MONOMER. ECOL316407:JW4057-MONOMER. MetaCyc:PHNL-MONOMER.
Gene expression databases
Genevestigator	P16679.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR012701. CP_lyase_PhnL. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF00005. ABC_tran. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR02324. CP_lyasePhnL. 1 hit.
PROSITE	PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHNL_ECOLI

Accession

Primary (citable) accession number: P16679
Secondary accession number(s): Q2M6K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 29, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program