Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyPhnH-like8034005 3001133 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyPhnH-like8034005 3001133 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF06754e4xb6A1 A: a+b two layersX: C-P lyase subunit PhnG (From Topology)H: C-P lyase subunit PhnG (From Topology)T: C-P lyase subunit PhnGF: PF06754ECOD (1.6)
EPF06754e4xb6E1 A: a+b two layersX: C-P lyase subunit PhnG (From Topology)H: C-P lyase subunit PhnG (From Topology)T: C-P lyase subunit PhnGF: PF06754ECOD (1.6)
BPF05845e4xb6B1 A: a/b three-layered sandwichesX: PhnH-like (From Topology)H: PhnH-like (From Topology)T: PhnH-likeF: PF05845ECOD (1.6)
FPF05845e4xb6F1 A: a/b three-layered sandwichesX: PhnH-like (From Topology)H: PhnH-like (From Topology)T: PhnH-likeF: PF05845ECOD (1.6)
CPF05861e4xb6C2 A: alpha arraysX: RuvA-CH: C-P lyase subunit PhnI N-terminal domain (From Topology)T: C-P lyase subunit PhnI N-terminal domainF: PF05861ECOD (1.6)
CPF05861e4xb6C1 A: a+b two layersX: C-P lyase subunit PhnG (From Topology)H: C-P lyase subunit PhnG (From Topology)T: C-P lyase subunit PhnGF: PF05861ECOD (1.6)
GPF05861e4xb6G2 A: alpha arraysX: RuvA-CH: C-P lyase subunit PhnI N-terminal domain (From Topology)T: C-P lyase subunit PhnI N-terminal domainF: PF05861ECOD (1.6)
GPF05861e4xb6G1 A: a+b two layersX: C-P lyase subunit PhnG (From Topology)H: C-P lyase subunit PhnG (From Topology)T: C-P lyase subunit PhnGF: PF05861ECOD (1.6)
DPF06007e4xb6D1 A: a/b three-layered sandwichesX: PhnH-like (From Topology)H: PhnH-like (From Topology)T: PhnH-likeF: PF06007ECOD (1.6)
DPF06007e4xb6D2 A: few secondary structure elementsX: C-P lyase subunit PhnJ C-terminal Zn-binding domain (From Topology)H: C-P lyase subunit PhnJ C-terminal Zn-binding domain (From Topology)T: C-P lyase subunit PhnJ C-terminal Zn-binding domainF: PF06007ECOD (1.6)
HPF06007e4xb6H2 A: a/b three-layered sandwichesX: PhnH-like (From Topology)H: PhnH-like (From Topology)T: PhnH-likeF: PF06007ECOD (1.6)
HPF06007e4xb6H1 A: few secondary structure elementsX: C-P lyase subunit PhnJ C-terminal Zn-binding domain (From Topology)H: C-P lyase subunit PhnJ C-terminal Zn-binding domain (From Topology)T: C-P lyase subunit PhnJ C-terminal Zn-binding domainF: PF06007ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B3.40.50.11310 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Bacterial phosphonate metabolism protein PhnHCATH (4.3.0)
F3.40.50.11310 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Bacterial phosphonate metabolism protein PhnHCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, E
PF06754Phosphonate metabolism protein PhnG (PhnG)Phosphonate metabolism protein PhnG- Family
B, F
PF05845Bacterial phosphonate metabolism protein (PhnH) (PhnH)Bacterial phosphonate metabolism protein (PhnH)- Family
C, G
PF05861Bacterial phosphonate metabolism protein (PhnI) (PhnI)Bacterial phosphonate metabolism protein (PhnI)- Family
D, H
PF06007Phosphonate metabolism protein PhnJ (PhnJ)Phosphonate metabolism protein PhnJ- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, E
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG
B, F
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH
C, G
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
D, H
Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase  M-CSA #949

This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate. The enzyme from the bacterium Escherichia coli can act on additional alpha-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. alpha-D-ribose-1- (N-(phosphonomethyl)glycine)-5-phosphate and alpha-D-ribose-1-(2-N- acetamidomethylphosphonate)-5-phosphate).

Defined by 5 residues: GLY:D-32CYS:D-241CYS:D-244CYS:D-266CYS:D-272
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Explore in 3DM-CSA Motif Definition
Extent of motif is too large to support Structure Motif searching.
EC: 4.7.1.1 (PDB Primary Data)