ID A0A0B5DZ74_9RHOB Unreviewed; 288 AA.
AC A0A0B5DZ74;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=P73_0812 {ECO:0000313|EMBL:AJE45527.1};
OS Celeribacter indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE45527.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE45527.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE45527.1};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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; CP004393; AJE45527.1; -; Genomic_DNA.
DR RefSeq; WP_043868584.1; NZ_FNNW01000008.1.
DR AlphaFoldDB; A0A0B5DZ74; -.
DR STRING; 1208324.P73_0812; -.
DR KEGG; cid:P73_0812; -.
DR HOGENOM; CLU_063386_0_0_5; -.
DR OrthoDB; 9803851at2; -.
DR Proteomes; UP000031521; 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, ECO:0000313|EMBL:AJE45527.1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR011468};
KW Reference proteome {ECO:0000313|Proteomes:UP000031521};
KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR011468}.
SQ SEQUENCE 288 AA; 32405 MW; BA6DE864060490F4 CRC64;
MSDYNFAYLD EQTKRMIRRA ILKGVAIPGY QVPFASREMP MPYGWGTGGV QVTAACLTPE
DRLKVIDQGA DDTTNAVSIR KFFERTAGVD TTERTGEATL IQTRHRIPEE PLTEGQILVY
QVPIPEPLRF LEPRETETRK MHALEDYGLM YVKLYEDISR HGHIATSYAY PVKVEERYVM
DPSPIPKFDN PKMEMAALQL FGAGREQRIY AVPPHTKVVS LDFEDHPFVA SKADHACDLC
GAEDSYLDEV IVDDAGGRMF VCSDTDYCAT RRASGHRGRM SPAEEAAE
//
