ID J3CZY6_9BRAD Unreviewed; 298 AA.
AC J3CZY6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ORFNames=PMI42_00332 {ECO:0000313|EMBL:EJN16114.1};
OS Bradyrhizobium sp. YR681.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1144344 {ECO:0000313|EMBL:EJN16114.1, ECO:0000313|Proteomes:UP000007272};
RN [1] {ECO:0000313|EMBL:EJN16114.1, ECO:0000313|Proteomes:UP000007272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR681 {ECO:0000313|EMBL:EJN16114.1,
RC ECO:0000313|Proteomes:UP000007272};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJN16114.1}.
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DR EMBL; AKIY01000009; EJN16114.1; -; Genomic_DNA.
DR RefSeq; WP_008129756.1; NZ_AKIY01000009.1.
DR AlphaFoldDB; J3CZY6; -.
DR PATRIC; fig|1144344.3.peg.222; -.
DR OrthoDB; 9803851at2; -.
DR Proteomes; UP000007272; Unassembled WGS sequence.
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 298 AA; 33146 MW; 8C0BC81CEDD73CB1 CRC64;
MNAPAYNFAY LDEQTKRMIR RAILKAIAIP GYQVPFASRE MPMPYGWGTG GVQVTAAILG
PSDVLKVIDQ GSDDTTNAIS IRKFFAKTAG VATTTATDEA TVIQTRHRIP ETSLHANQVL
VYQVPIPEPL RFLEPRETET RRMHALAEYG LMHVKLYEDI ARFGHIATAY AYPVKVNARY
VMDPSPTPKF DNPKMDNCPA LQLFGAGREK RIYAIPPYTQ VVSLDFEDHP FEPYRFNAPC
ALCAAENSYL DEIVTDDKGG RMFVCSDTDY CEGRQAAGHH GSLSAAPYKE KAQEKSNG
//
