ID Q2ISM5_RHOP2 Unreviewed; 293 AA.
AC Q2ISM5;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase {ECO:0000256|PIRNR:PIRNR011468};
DE Short=PRPn C-P lyase {ECO:0000256|PIRNR:PIRNR011468};
DE EC=4.7.1.1 {ECO:0000256|PIRNR:PIRNR011468};
GN OrderedLocusNames=RPB_4092 {ECO:0000313|EMBL:ABD08785.1};
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD08785.1, ECO:0000313|Proteomes:UP000008809};
RN [1] {ECO:0000313|EMBL:ABD08785.1, ECO:0000313|Proteomes:UP000008809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2 {ECO:0000313|EMBL:ABD08785.1,
RC ECO:0000313|Proteomes:UP000008809};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the breakage of the C-P bond in alpha-D-ribose 1-
CC methylphosphonate 5-phosphate (PRPn) forming alpha-D-ribose.
CC {ECO:0000256|PIRNR:PIRNR011468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + alpha-D-ribose 1-methylphosphonate 5-phosphate + S-
CC adenosyl-L-methionine = 5'-deoxyadenosine + A + alpha-D-ribose 1,2-
CC cyclic phosphate 5-phosphate + H(+) + L-methionine + methane;
CC Xref=Rhea:RHEA:34707, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16183, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:68686,
CC ChEBI:CHEBI:68687; EC=4.7.1.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR011468};
CC -!- SIMILARITY: Belongs to the PhnJ family.
CC {ECO:0000256|PIRNR:PIRNR011468}.
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DR EMBL; CP000250; ABD08785.1; -; Genomic_DNA.
DR RefSeq; WP_011442969.1; NC_007778.1.
DR AlphaFoldDB; Q2ISM5; -.
DR STRING; 316058.RPB_4092; -.
DR KEGG; rpb:RPB_4092; -.
DR eggNOG; COG3627; Bacteria.
DR HOGENOM; CLU_063386_0_0_5; -.
DR OrthoDB; 9803851at2; -.
DR Proteomes; UP000008809; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0098848; F:alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019700; P:organic phosphonate catabolic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR010306; PhnJ.
DR Pfam; PF06007; PhnJ; 1.
DR PIRSF; PIRSF011468; PhnJ; 1.
DR SFLD; SFLDF00379; Phosphonate_metabolism_(PhnJ); 1.
DR SFLD; SFLDG01115; Phosphonate_metabolism_(PhnJ); 1.
DR SFLD; SFLDS00033; Radical_SAM_Phosphonate_Metabo; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR011468};
KW Iron {ECO:0000256|PIRNR:PIRNR011468};
KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR011468};
KW Lyase {ECO:0000256|PIRNR:PIRNR011468};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR011468};
KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR011468}.
SQ SEQUENCE 293 AA; 32894 MW; B9C6085C4752B793 CRC64;
MNAPQYNFAY LDEQTKRMIR RAILKAIAIP GYQVPFASRE MPMPYGWGTG GVQVTAAILG
PDDVLKVIDQ GSDDTTNAIS IRKFFAKTAG VATTTSTTDA SVIQTRHRIP EAPLHEGQVL
VYQVPIPEPL RFLEPRETET RRMHALAEYG LMHVKLYEDI AKFGHIATSY AYPVKVNSRY
VMDPSPTPKF DNPKMDDCPA LQLFGAGREK RIYAIPPYTH VVSLDFQDHP FTRYRQDAPC
ALCGSEESYL DEIVTDDRGG RMFVCSDTDY CETRQVQGHR GSESAPHQER ADA
//
