P16688

PR
Gene name
phnJ (b4098, JW4059)
Protein name
Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase
Names
PRPn C-P lyase
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b4098
EC number
4.7.1.1: Carbon-phosphorus lyases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

64-135 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

7 structures for P16688

Entry ID Method Resolution Chain Position Source
4XB6 X-ray 170 A D/H 1-281 PDB
7Z15 EM 193 A D/H 1-281 PDB
7Z16 EM 209 A D/H 1-281 PDB
7Z17 EM 257 A D/H 1-281 PDB
7Z18 EM 198 A D/H 1-281 PDB
7Z19 EM 257 A D/H 1-281 PDB
AF-P16688-F1 Predicted AlphaFoldDB

1 variants for P16688

Variant ID(s) Position Change Description Diseaes Association Provenance
103 V>L strain: B [UniProt] No

No associated diseases with P16688

No regional properties for P16688

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P16688

Functions

Description
EC Number 4.7.1.1 Carbon-phosphorus lyases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex A catalytic protein complex that is capable of alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activity.
carbon phosphorus lyase complex A protein complex which is capable of carbon phosphorus lyase activity.

4 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase activity Catalysis of the reaction: alpha-D-ribose 1-methylphosphonate 5-phosphate = alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + methane.
lyase activity Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
metal ion binding Binding to a metal ion.

3 GO annotations of biological process

Name Definition
organic phosphonate catabolic process The chemical reactions and pathways resulting in the breakdown of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Catabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
organic phosphonate metabolic process The chemical reactions and pathways involving phosphonates, any organic compounds containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Metabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
organic phosphonate transport The directed movement of phosphonates into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. A phosphonate is any salt, anion, or ester of phosphonic acid (HPO(OH)2).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MANLSGYNFA YLDEQTKRMI RRAILKAVAI PGYQVPFGGR EMPMPYGWGT GGIQLTASVI
70 80 90 100 110 120
GESDVLKVID QGADDTTNAV SIRNFFKRVT GVNTTERTDD ATVIQTRHRI PETPLTEDQI
130 140 150 160 170 180
IIFQVPIPEP LRFIEPRETE TRTMHALEEY GVMQVKLYED IARFGHIATT YAYPVKVNGR
190 200 210 220 230 240
YVMDPSPIPK FDNPKMDMMP ALQLFGAGRE KRIYAVPPFT RVESLDFDDH PFTVQQWDEP
250 260 270 280
CAICGSTHSY LDEVVLDDAG NRMFVCSDTD YCRQQSEAKN Q