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Database: UniProt
Entry: V8G9X6_9BURK
LinkDB: V8G9X6_9BURK
Original site: V8G9X6_9BURK 
ID   V8G9X6_9BURK            Unreviewed;       293 AA.
AC   V8G9X6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   03-MAY-2023, entry version 24.
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=V757_04090 {ECO:0000313|EMBL:ETD72477.1};
OS   Pelistega indica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pelistega.
OX   NCBI_TaxID=1414851 {ECO:0000313|EMBL:ETD72477.1, ECO:0000313|Proteomes:UP000018766};
RN   [1] {ECO:0000313|EMBL:ETD72477.1, ECO:0000313|Proteomes:UP000018766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HM-7 {ECO:0000313|EMBL:ETD72477.1,
RC   ECO:0000313|Proteomes:UP000018766};
RA   Kumbhare S.V., Shetty S.A., Sharma O., Dhotre D.P.;
RT   "Genomic analysis of Pelistega sp. HM-7.";
RL   Submitted (NOV-2013) 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   -!- 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:ETD72477.1}.
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DR   EMBL; AYSV01000065; ETD72477.1; -; Genomic_DNA.
DR   AlphaFoldDB; V8G9X6; -.
DR   PATRIC; fig|1414851.3.peg.820; -.
DR   Proteomes; UP000018766; 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, ECO:0000313|EMBL:ETD72477.1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR011468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018766};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR011468}.
SQ   SEQUENCE   293 AA;  33117 MW;  538CCFC4661CD559 CRC64;
     MSSTQTKPID NAYNFAYLDE QTKRMLRRCL LKAVAIPGYQ VPFGGREMPL PYGWGTGGMQ
     VTAAILGQDD VLKVIDQGAD DTTNAVSIRH FFERTAGVNT TEKTELATII QTRHRIPEKA
     LKEDQIMVFQ VPIPEPLRFI EPSETETKTM HALNDYGVMH VKLYEDIARF GHIATAYAYP
     VLVNDRYVMD PSPIPKFDNP KLDKSPALML FGAGREKRLY AVPPFTEVQS LDFEDHPFTV
     QQWDHACDIC GSRHSFLDEL ITDDQGGRSY VCSDTDYCAE QVAKKSVEQQ EDK
//
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