ID B6BC47_9RHOB Unreviewed; 285 AA.
AC B6BC47;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 Name=phnJ {ECO:0000313|EMBL:EDZ48147.1};
GN ORFNames=RBY4I_3367 {ECO:0000313|EMBL:EDZ48147.1};
OS Rhodobacterales bacterium Y4I.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ48147.1, ECO:0000313|Proteomes:UP000005133};
RN [1] {ECO:0000313|EMBL:EDZ48147.1, ECO:0000313|Proteomes:UP000005133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y4I {ECO:0000313|EMBL:EDZ48147.1,
RC ECO:0000313|Proteomes:UP000005133};
RA Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995281; EDZ48147.1; -; Genomic_DNA.
DR AlphaFoldDB; B6BC47; -.
DR STRING; 439496.RBY4I_3367; -.
DR eggNOG; COG3627; Bacteria.
DR HOGENOM; CLU_063386_0_0_5; -.
DR OrthoDB; 9803851at2; -.
DR Proteomes; UP000005133; 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 Reference proteome {ECO:0000313|Proteomes:UP000005133};
KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR011468}.
SQ SEQUENCE 285 AA; 31903 MW; 2DB029DCBBB1B977 CRC64;
MNDYNFAYLD EQTKRMIRRA ILKGLAVPGY QVPFASREMP MPYGWGTGGV QVSAATLTPD
DTLKVIDQGA DDTTNAVSIR KFFEKTAGVA TTEETAKASV IQTRHRIPEA ELTEDQILVY
QVPIPEPLRF LEPRETETRK MHSLQEYGLM HVKLYEDISQ HGAIATAYAY PVKVEGRYVM
DPSPIPKFDN PKMEMAAIQL FGAGREQRIY AVPPFTQVVS LDFEDYPFEA SKADHPCDLC
AAEDSYLDEV ILDDAGNRMF VCSDTDYCRT RRDAGHTGRL GEGAA
//
