Entry
Name
alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase;
phnJ (gene name)
Class
Lyases;
carbon-phosphorus lyases;
carbon-phosphorus lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
alpha-D-ribose-1-methylphosphonate-5-phosphate C-P-lyase (methane-forming)
Reaction(IUBMB)
alpha-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine + reduced electron acceptor = alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + methane + L-methionine + 5'-deoxyadenosine + oxidized electron acceptor [RN:
R10204 ]
Reaction(KEGG)
Substrate
alpha-D-ribose 1-methylphosphonate 5-phosphate [CPD:
C20423 ];
S-adenosyl-L-methionine [CPD:
C00019 ];
reduced electron acceptor
Product
alpha-D-ribose 1,2-cyclic phosphate 5-phosphate [CPD:
C20440 ];
methane [CPD:
C01438 ];
L-methionine [CPD:
C00073 ];
5'-deoxyadenosine [CPD:
C05198 ];
oxidized electron acceptor
Comment
This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate. Contains an [4Fe-4S] cluster. The enzyme from the bacterium Escherichia coli can act on additional alpha-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. alpha-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and alpha-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).
History
EC 4.7.1.1 created 2013, modified 2016
Pathway
ec00440 Phosphonate and phosphinate metabolism
Orthology
K06163 alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase
Genes
ECOO : ECRM13514_5314(phnJ)
ECOH : ECRM13516_4982(phnJ)
ECW : EcE24377A_4652(phnJ)
EDJ : ECDH1ME8569_3957(phnJ)
REE : electrica_04694(phnJ)
BAGE : BADSM9389_38170(phnJ)
YPG : YpAngola_A4028(phnJ)
YPI : YpsIP31758_3563(phnJ)
SMW : SMWW4_v1c04610(phnJ)
PCC : PCC21_005070 PCC21_009150
PPOA : BJK05_19445 BJK05_21500
PARI : I2D83_17520 I2D83_19335
VPL : SA104470976_00033(phnJ)
PAEB : NCGM1900_2895(phnJ)
PAEU : BN889_03751(phnJ_1)
PVD : CFBP1590__3162(phnJ)
MAQ : Maqu_0220 Maqu_2292 Maqu_4040 Maqu_4146
BMV : BMASAVP1_A0319(phnJ)
BML : BMA10229_A1180(phnJ)
BPL : BURPS1106A_3342(phnJ)
BUE : BRPE67_BCDS01880(phnJ)
PDIO : PDMSB3_0927.1(phnJ)
BUO : BRPE64_BCDS02010(phnJ)
MPT : Mpe_B0427(htxI) Mpe_B0463(htxI)
MLO : mll9152 mlr3346 mlr9282
MOH : IHQ72_09160 IHQ72_32275
SMEL : SM2011_b20762(phnJ)
SFD : USDA257_c15730(phnJ)
SAME : SAMCFNEI73_pC0531(phnJ)
EMX : FKV68_18720 FKV68_24065 FKV68_26505
AGR : AGROH133_03153(phnJ)
AGC : BSY240_3014 BSY240_41
AVV : RvVAT039_18770(phnJ)
AVF : RvVAR031_05940(phnJ) RvVAR031_pl06670(phnJ)
REC : RHECIAT_CH0000208(phnJ)
REL : REMIM1_CH00172(phnJ)
REP : IE4803_CH00184(phnJ)
REI : IE4771_CH00184(phnJ)
RTR : RTCIAT899_CH01050(phnJ)
RGA : RGR602_CH00185(phnJ)
RPHA : AMC79_CH00213(phnJ)
RJG : CCGE525_01300 CCGE525_02010
RHR : CKA34_04045 CKA34_25295
RHIB : I8E17_18070 I8E17_25075
NGL : RG1141_CH42940(phnJ)
NEN : NCHU2750_39240(phnJ)
NPM : QEO92_24835 QEO92_25815
BEL : BE61_02050(phnJ) BE61_75160(phnJ)
BAUT : QA635_04245 QA635_30985
BCOU : IC761_04420 IC761_30705
VGO : GJW-30_1_01645(phnJ)
MAQU : Maq22A_c06550(phnJ)
PPHR : APZ00_04500 APZ00_19590
RLI : RLO149_c016810(phnJ)
PHP : PhaeoP97_02928(phnJ)
PPIC : PhaeoP14_00344(phnJ)
CON : TQ29_11145 TQ29_11350
PABY : Ga0080574_TMP3559 Ga0080574_TMP3637
SINL : DSM14862_02372(phnJ)
SPSE : SULPSESMR1_00533(phnJ) SULPSESMR1_03694(phnJ)
RMM : ROSMUCSMR3_01313(phnJ)
RID : RIdsm_00555(phnJ_1) RIdsm_05992(phnJ_2)
AHT : ANTHELSMS3_00439 ANTHELSMS3_02922
PARS : DRW48_02335 DRW48_06985
DAA : AKL17_2162 AKL17_3365
LVS : LOKVESSMR4R_00412(phnJ) LOKVESSMR4R_01954(phnJ) LOKVESSMR4R_03845(phnJ)
TAW : EI545_05190 EI545_16415
HML : HmaOT1_13535 HmaOT1_19715 HmaOT1_19840
DMS : E8L03_02895 E8L03_15925
PTHE : LF599_08875 LF599_17075
COHN : KCTCHS21_53280(phnJ)
AFAS : NZD89_12525 NZD89_12580
PDF : CD630DERM_35350(phnJ)
PFAC : PFJ30894_00327(phnJ)
AARG : Aargi30884_26050(phnJ)
ABSI : A9CBEGH2_23370(phnJ)
RTS : CE91St31_31540(phnJ)
MPHL : MPHLCCUG_02257(phnJ)
FSB : GCM10025867_36660(phnJ)
CALL : OZ401_002718 OZ401_002731
» show all
Taxonomy
Reference
Authors
Kamat SS, Williams HJ, Raushel FM
Title
Intermediates in the transformation of phosphonates to phosphate by bacteria.
Journal
Sequence
Reference
Authors
Jochimsen B, Lolle S, McSorley FR, Nabi M, Stougaard J, Zechel DL, Hove-Jensen B
Title
Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway.
Journal
Reference
Authors
Zhang Q, van der Donk WA
Title
Answers to the carbon-phosphorus lyase conundrum.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 4.7.1.1
ExPASy - ENZYME nomenclature database: 4.7.1.1
BRENDA, the Enzyme Database: 4.7.1.1