XECA_XANP2
ID XECA_XANP2 Reviewed; 376 AA.
AC Q56837; A7IPY0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=2-hydroxypropyl-CoM lyase {ECO:0000305};
DE EC=4.4.1.23 {ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:11939797};
DE AltName: Full=Aliphatic epoxide carboxylation component I;
DE AltName: Full=Epoxide carboxylase component I {ECO:0000303|PubMed:9405410};
DE AltName: Full=Epoxyalkane:CoM transferase {ECO:0000303|PubMed:10411892};
DE Short=EaCoMT {ECO:0000303|PubMed:11939797};
GN Name=xecA1 {ECO:0000303|PubMed:12524213}; OrderedLocusNames=Xaut_4865;
GN and
GN Name=xecA2 {ECO:0000303|PubMed:12524213}; OrderedLocusNames=Xaut_5047;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG Plasmid pXAUT01.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RX PubMed=7704278; DOI=10.1099/13500872-141-2-477;
RA Swaving J., Weijers C.A.G.M., van Ooyen A.J.J., de Bont J.A.M.;
RT "Complementation of Xanthobacter Py2 mutants in epoxyalkane degradation;
RT expression and nucleotide sequence of the complementing DNA fragment.";
RL Microbiology 141:477-484(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of plasmid pXAUT01 of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-12, FUNCTION, COFACTOR, ACTIVITY REGULATION, PATHWAY,
RP AND SUBUNIT.
RC STRAIN=ATCC BAA-1158 / Py2;
RX PubMed=9405410; DOI=10.1074/jbc.272.51.32121;
RA Allen J.R., Ensign S.A.;
RT "Purification to homogeneity and reconstitution of the individual
RT components of the epoxide carboxylase multiprotein enzyme complex from
RT Xanthobacter strain Py2.";
RL J. Biol. Chem. 272:32121-32128(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC BAA-1158 / Py2;
RX PubMed=10411892; DOI=10.1073/pnas.96.15.8432;
RA Allen J.R., Clark D.D., Krum J.G., Ensign S.A.;
RT "A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial
RT pathway of aliphatic epoxide carboxylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8432-8437(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-220.
RC STRAIN=ATCC BAA-1158 / Py2;
RX PubMed=11939797; DOI=10.1021/bi0255221;
RA Krum J.G., Ellsworth H., Sargeant R.R., Rich G., Ensign S.A.;
RT "Kinetic and microcalorimetric analysis of substrate and cofactor
RT interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase.";
RL Biochemistry 41:5005-5014(2002).
RN [6]
RP ACTIVITY REGULATION.
RC STRAIN=ATCC BAA-1158 / Py2;
RX PubMed=20551308; DOI=10.1074/jbc.m110.144410;
RA Boyd J.M., Clark D.D., Kofoed M.A., Ensign S.A.;
RT "Mechanism of inhibition of aliphatic epoxide carboxylation by the coenzyme
RT M analog 2-bromoethanesulfonate.";
RL J. Biol. Chem. 285:25232-25242(2010).
RN [7]
RP REVIEW.
RX PubMed=12524213; DOI=10.1146/annurev.biochem.72.121801.161820;
RA Ensign S.A., Allen J.R.;
RT "Aliphatic epoxide carboxylation.";
RL Annu. Rev. Biochem. 72:55-76(2003).
CC -!- FUNCTION: Involved in aliphatic epoxide carboxylation (PubMed:9405410,
CC PubMed:10411892, PubMed:11939797). Catalyzes the addition of coenzyme M
CC (CoM) to either R- or S-epoxypropane to form the thioether conjugate 2-
CC hydroxypropyl-CoM (PubMed:10411892, PubMed:11939797). Catalyzes the
CC reaction of CoM with R-epoxypropane at a rate approximately twice of
CC that with S-epoxypropane (PubMed:10411892). The CoM analogs 2-
CC mercaptopropionate, 2-mercaptoethanol and cysteine substitute poorly
CC for CoM as the thiol substrate (PubMed:11939797).
CC {ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:11939797,
CC ECO:0000269|PubMed:9405410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-2-hydroxypropyl-coenzyme M = (R)-1,2-epoxypropane +
CC coenzyme M; Xref=Rhea:RHEA:19421, ChEBI:CHEBI:28985,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58458; EC=4.4.1.23;
CC Evidence={ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:11939797};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19423;
CC Evidence={ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:11939797};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxypropyl-coenzyme M = (S)-1,2-epoxypropane +
CC coenzyme M; Xref=Rhea:RHEA:20904, ChEBI:CHEBI:28982,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58430; EC=4.4.1.23;
CC Evidence={ECO:0000269|PubMed:10411892};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20906;
CC Evidence={ECO:0000269|PubMed:10411892};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11939797, ECO:0000269|PubMed:9405410};
CC Note=Binds 1 zinc ion per subunit (PubMed:9405410, PubMed:11939797).
CC Zinc plays a key role in activating an organic thiol substrate for
CC nucleophilic attack on an alkyl-donating substrate (PubMed:11939797).
CC {ECO:0000269|PubMed:11939797, ECO:0000269|PubMed:9405410};
CC -!- ACTIVITY REGULATION: Inhibited by methylepoxypropane (PubMed:9405410).
CC Inhibited by the zinc chelator 4-(2-pyridylazo)resorcinol (PAR), in the
CC presence of p- (hydroxymercuri)benzenesulfonic acid (PMPS), and by EDTA
CC (PubMed:11939797). Not inhibited by the coenzyme M analog 2-
CC bromoethanesulfonate (BES) (PubMed:20551308).
CC {ECO:0000269|PubMed:11939797, ECO:0000269|PubMed:20551308,
CC ECO:0000269|PubMed:9405410}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for R-epoxypropane {ECO:0000269|PubMed:11939797};
CC KM=33.6 uM for coenzyme M {ECO:0000269|PubMed:11939797};
CC Note=kcat is 6.5 sec(-1) with R-epoxypropane as substrate.
CC {ECO:0000269|PubMed:11939797};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:11939797};
CC -!- PATHWAY: Alkene metabolism; propylene degradation.
CC {ECO:0000269|PubMed:10411892, ECO:0000269|PubMed:9405410}.
CC -!- SUBUNIT: Homohexamer (PubMed:9405410). Component I of the aliphatic
CC epoxide carboxylation complex together with components II, III and IV
CC (PubMed:9405410, PubMed:10411892). {ECO:0000269|PubMed:10411892,
CC ECO:0000269|PubMed:9405410}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000305}.
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DR EMBL; X79863; CAA56241.1; -; Genomic_DNA.
DR EMBL; CP000782; ABS70076.1; -; Genomic_DNA.
DR EMBL; CP000782; ABS70245.1; -; Genomic_DNA.
DR PIR; S47051; S47051.
DR RefSeq; WP_011992980.1; NC_009717.1.
DR AlphaFoldDB; Q56837; -.
DR SMR; Q56837; -.
DR STRING; 78245.Xaut_4865; -.
DR EnsemblBacteria; ABS70076; ABS70076; Xaut_4865.
DR EnsemblBacteria; ABS70245; ABS70245; Xaut_5047.
DR KEGG; xau:Xaut_4865; -.
DR KEGG; xau:Xaut_5047; -.
DR eggNOG; COG0620; Bacteria.
DR HOGENOM; CLU_040013_3_0_5; -.
DR OMA; DPDCGMR; -.
DR OrthoDB; 577156at2; -.
DR PhylomeDB; Q56837; -.
DR BioCyc; MetaCyc:MON-7713; -.
DR UniPathway; UPA00776; -.
DR Proteomes; UP000002417; Plasmid pXAUT01.
DR GO; GO:0050555; F:2-hydroxypropyl-CoM lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR GO; GO:0042208; P:propylene catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 1.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR Pfam; PF01717; Meth_synt_2; 2.
DR SUPFAM; SSF51726; SSF51726; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Metal-binding; Plasmid;
KW Reference proteome; Zinc.
FT CHAIN 1..376
FT /note="2-hydroxypropyl-CoM lyase"
FT /id="PRO_0000098705"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:11939797"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MUTAGEN 220
FT /note="C->A: Retains 0.06% of wild-type specific activity.
FT Decreased binding affinity for CoM."
FT /evidence="ECO:0000269|PubMed:11939797"
SQ SEQUENCE 376 AA; 41690 MW; FB47C74670C6748B CRC64;
MLIRGEDVTI PTSMVGNYPN PRWWDAQFAR TWTGDQEPPD ALIQESLEDA VAAIARDQER
AGLDIISDGR VHGDNYAEQA LYYYYRRLGY DLKGGYLGFP IYSRLHAGTL TGEVRRHGAI
MVEQAKALKK ATGKPTKVQY TGVQALTQAT NDLHYKSSRD RAMAIAKAIN EDIREVDALG
VDFIQIDEFT WPYFFEDWAI EAFNAAVDGV KNAKIIAHVC WGNWGGTPAY YPDETAASGE
IFDLTKRKAE ATKATATGSI VPKAYEARLD VLNLESCGRR SDDLSGLHVM KNHPLPDNVS
FWAGVIDVKS TITETADEVA NRIRRLLEIV PADRLGVTTD CGLILLQRYI AQDKLHALVE
GTKIVRAELA KAKQAA
