MCRA_METTM
ID MCRA_METTM Reviewed; 550 AA.
AC P11558; D9PY29;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Methyl-coenzyme M reductase I subunit alpha {ECO:0000303|PubMed:2269306};
DE Short=MCR I alpha {ECO:0000303|PubMed:2269306};
DE EC=2.8.4.1 {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha;
GN Name=mcrA; OrderedLocusNames=MTBMA_c15480;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=2448287; DOI=10.1128/jb.170.2.568-577.1988;
RA Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.;
RT "Cloning and characterization of the methyl coenzyme M reductase genes from
RT Methanobacterium thermoautotrophicum.";
RL J. Bacteriol. 170:568-577(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [3]
RP PROTEIN SEQUENCE OF 2-19, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND DEVELOPMENTAL STAGE.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=2269306; DOI=10.1111/j.1432-1033.1990.tb19481.x;
RA Rospert S., Linder D., Ellermann J., Thauer R.K.;
RT "Two genetically distinct methyl-coenzyme M reductases in Methanobacterium
RT thermoautotrophicum strain Marburg and delta H.";
RL Eur. J. Biochem. 194:871-877(1990).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, COFACTOR, ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=3350018; DOI=10.1111/j.1432-1033.1988.tb13941.x;
RA Ellermann J., Hedderich R., Boecher R., Thauer R.K.;
RT "The final step in methane formation. Investigations with highly purified
RT methyl-CoM reductase (component C) from Methanobacterium
RT thermoautotrophicum (strain Marburg).";
RL Eur. J. Biochem. 172:669-677(1988).
RN [5]
RP COFACTOR.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=9030728; DOI=10.1111/j.1432-1033.1997.00110.x;
RA Goubeaud M., Schreiner G., Thauer R.K.;
RT "Purified methyl-coenzyme-M reductase is activated when the enzyme-bound
RT coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III)
RT citrate.";
RL Eur. J. Biochem. 243:110-114(1997).
RN [6]
RP METHYLATION AT HIS-257; ARG-271; GLN-400 AND CYS-452, AND THIOCARBOXYLATION
RP AT GLY-445.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=10660523; DOI=10.1074/jbc.275.6.3755;
RA Selmer T., Kahnt J., Goubeaud M., Shima S., Grabarse W., Ermler U.,
RA Thauer R.K.;
RT "The biosynthesis of methylated amino acids in the active site region of
RT methyl-coenzyme M reductase.";
RL J. Biol. Chem. 275:3755-3760(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=23533332; DOI=10.1155/2013/920241;
RA Wrede C., Walbaum U., Ducki A., Heieren I., Hoppert M.;
RT "Localization of methyl-Coenzyme M reductase as metabolic marker for
RT diverse methanogenic Archaea.";
RL Archaea 2013:920241-920241(2013).
RN [8]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=25691570; DOI=10.1074/jbc.m115.636761;
RA Wongnate T., Ragsdale S.W.;
RT "The reaction mechanism of methyl-coenzyme M reductase: how an enzyme
RT enforces strict binding order.";
RL J. Biol. Chem. 290:9322-9334(2015).
RN [9] {ECO:0007744|PDB:1MRO}
RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-549 IN COMPLEX WITH COENZYME
RP F430; COENZYME B; COENZYME M AND MCR SUBUNITS BETA AND GAMMA, METHYLATION
RP AT HIS-257; ARG-271; GLN-400 AND CYS-452, THIOCARBOXYLATION AT GLY-445,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=9367957; DOI=10.1126/science.278.5342.1457;
RA Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.;
RT "Crystal structure of methyl-coenzyme M reductase: the key enzyme of
RT biological methane formation.";
RL Science 278:1457-1462(1997).
RN [10] {ECO:0007744|PDB:1HBM, ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1HBO, ECO:0007744|PDB:1HBU}
RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 2-550 IN COMPLEXES WITH
RP COM-S-S-COB; COENZYME B; COENZYME F430; COENZYME M AND MCR SUBUNITS BETA
RP AND GAMMA, METHYLATION AT HIS-257; ARG-271; GLN-400 AND CYS-452, AND
RP THIOCARBOXYLATION AT GLY-445.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=11491299; DOI=10.1006/jmbi.2001.4647;
RA Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., Thauer R.K.,
RA Lamzin V., Ermler U.;
RT "On the mechanism of biological methane formation: structural evidence for
RT conformational changes in methyl-coenzyme M reductase upon substrate
RT binding.";
RL J. Mol. Biol. 309:315-330(2001).
RN [11] {ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3M2R, ECO:0007744|PDB:3M2U, ECO:0007744|PDB:3M2V, ECO:0007744|PDB:3M30, ECO:0007744|PDB:3M32}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-550 IN COMPLEXES WITH
RP COM-S-S-COB; COENZYME B; COENZYME F430; COENZYME M; COENZYME B ANALOGS AND
RP MCR SUBUNITS BETA AND GAMMA, METHYLATION AT HIS-257; ARG-271; GLN-400 AND
RP CYS-452, AND THIOCARBOXYLATION AT GLY-445.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20707311; DOI=10.1021/bi100458d;
RA Cedervall P.E., Dey M., Pearson A.R., Ragsdale S.W., Wilmot C.M.;
RT "Structural insight into methyl-coenzyme M reductase chemistry using
RT coenzyme B analogues.";
RL Biochemistry 49:7683-7693(2010).
RN [12] {ECO:0007744|PDB:3POT}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH COENZYME F430;
RP COENZYME B; COENZYME M AND MCR SUBUNITS BETA AND GAMMA, METHYLATION AT
RP HIS-257; ARG-271; GLN-400 AND CYS-452, AND THIOCARBOXYLATION AT GLY-445.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=21438550; DOI=10.1021/ja110492p;
RA Cedervall P.E., Dey M., Li X., Sarangi R., Hedman B., Ragsdale S.W.,
RA Wilmot C.M.;
RT "Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase
RT from Methanothermobacter marburgensis.";
RL J. Am. Chem. Soc. 133:5626-5628(2011).
RN [13] {ECO:0007744|PDB:5A0Y}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH COENZYME F430;
RP COENZYME B; COENZYME M AND MCR SUBUNITS BETA AND GAMMA, METHYLATION AT
RP HIS-257; ARG-271; GLN-400 AND CYS-452, THIOCARBOXYLATION AT GLY-445, AND
RP DEHYDROGENATION AT ASP-450.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=27467699; DOI=10.1002/anie.201603882;
RA Wagner T., Kahnt J., Ermler U., Shima S.;
RT "Didehydroaspartate Modification in Methyl-CoenzymeM Reductase Catalyzing
RT Methane Formation.";
RL Angew. Chem. Int. Ed. Engl. 55:10630-10633(2016).
RN [14] {ECO:0007744|PDB:5G0R}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH COENZYME B; COENZYME
RP F430 AND MCR SUBUNITS BETA AND GAMMA, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=27140643; DOI=10.1073/pnas.1600298113;
RA Duin E.C., Wagner T., Shima S., Prakash D., Cronin B., Yanez-Ruiz D.R.,
RA Duval S., Rumbeli R., Stemmler R.T., Thauer R.K., Kindermann M.;
RT "Mode of action uncovered for the specific reduction of methane emissions
RT from ruminants by the small molecule 3-nitrooxypropanol.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:6172-6177(2016).
CC -!- FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that
CC catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-
CC (methylthio)ethanesulfonate) using coenzyme B (CoB or 7-
CC mercaptoheptanoylthreonine phosphate) as reductant which results in the
CC production of methane and the mixed heterodisulfide of CoB and CoM
CC (CoM-S-S-CoB). This is the final step in methanogenesis
CC (PubMed:2269306, PubMed:3350018, PubMed:27140643). Neither N-6-
CC mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8-
CC mercaptooctanoylthreonine phosphate (H-SOcoTP) nor any other thiol
CC compound such as CoA or CoM can substitute for CoB as the electron
CC donor (PubMed:3350018). {ECO:0000269|PubMed:2269306,
CC ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B
CC heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183,
CC ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1;
CC Evidence={ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570,
CC ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC Evidence={ECO:0000269|PubMed:27140643, ECO:0000305|PubMed:3350018};
CC -!- COFACTOR:
CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC Evidence={ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728,
CC ECO:0000269|PubMed:9367957};
CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957).
CC Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme
CC F430 is reduced to the Ni(I) oxidation state (PubMed:9030728).
CC {ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728,
CC ECO:0000269|PubMed:9367957};
CC -!- ACTIVITY REGULATION: Methyl-coenzyme M reductase activity is inhibited
CC by 3-nitrooxypropanol (3-NOP) in vitro and in vivo, by oxidation of its
CC active site Ni(I), which stops both growth and methanogenesis
CC (PubMed:27140643). Is also inhibited by the reaction product CoM-S-S-
CC CoB (PubMed:3350018). {ECO:0000269|PubMed:27140643,
CC ECO:0000269|PubMed:3350018}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for coenzyme B {ECO:0000269|PubMed:2269306,
CC ECO:0000269|PubMed:3350018};
CC KM=4 mM for methyl-coenzyme M {ECO:0000269|PubMed:2269306,
CC ECO:0000269|PubMed:3350018};
CC KM=169 uM for coenzyme B (at 25 degrees Celsius, under conditions in
CC which the heterodisulfide product is recycled via reduction by
CC hydroxocobalamin) {ECO:0000269|PubMed:25691570};
CC KM=42 uM for coenzyme B (at 25 degrees Celsius, under conditions in
CC which the heterodisulfide product is not recycled)
CC {ECO:0000269|PubMed:25691570};
CC Vmax=40 nmol/min/mg enzyme {ECO:0000269|PubMed:3350018};
CC Vmax=7.8 umol/min/mg enzyme (at 25 degrees Celsius, under conditions
CC in which the heterodisulfide product is recycled via reduction by
CC hydroxocobalamin) {ECO:0000269|PubMed:25691570};
CC Vmax=0.41 umol/min/mg enzyme (at 25 degrees Celsius, under conditions
CC in which the heterodisulfide product is not recycled)
CC {ECO:0000269|PubMed:25691570};
CC Note=kcat is 18 sec(-1) (at 25 degrees Celsius, under conditions in
CC which the heterodisulfide product is recycled via reduction by
CC hydroxocobalamin). kcat is 0.96 sec(-1) (at 25 degrees Celsius, under
CC conditions in which the heterodisulfide product is not recycled).
CC {ECO:0000269|PubMed:25691570};
CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC from methyl-coenzyme M: step 1/1. {ECO:0000269|PubMed:27140643,
CC ECO:0000269|PubMed:3350018}.
CC -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains,
CC forming a dimer of heterotrimers. {ECO:0000269|PubMed:2269306,
CC ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9367957}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23533332}.
CC Note=Under growth limiting conditions on nickel-depleted media, a
CC fraction of 70% of the enzyme is localized close to the cytoplasmic
CC membrane, which implies 'facultative' membrane association of the
CC enzyme. {ECO:0000269|PubMed:23533332}.
CC -!- DEVELOPMENTAL STAGE: There are two MCR complexes in this bacteria. MCR
CC II is expressed in the early growth phase. Late growth cells contain
CC mostly MCR I. {ECO:0000269|PubMed:2269306}.
CC -!- PTM: The alpha subunit contains six modified amino acids near the
CC active site region (PubMed:27467699). Is methylated on His-257, Arg-
CC 271, Gln-400 and Cys-452, probably by the action of specific S-
CC adenosylmethionine-dependent methyltransferases. Also contains a
CC thioglycine at position 445, forming a thiopeptide bond
CC (PubMed:10660523, PubMed:9367957, PubMed:11491299, PubMed:20707311,
CC PubMed:21438550, PubMed:27467699). Contains a didehydroaspartate
CC residue at position 450 (PubMed:27467699). The methylation on C5 of
CC Arg-271 is a post-translational methylation not essential in vivo, but
CC which plays a role for the stability and structural integrity of MCR
CC (By similarity). {ECO:0000250|UniProtKB:Q8THH1,
CC ECO:0000269|PubMed:10660523, ECO:0000269|PubMed:11491299,
CC ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550,
CC ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957}.
CC -!- MISCELLANEOUS: The MCR reaction has been shown to follow an ordered bi-
CC bi ternary complex mechanism, in which methyl-SCoM must enter the MCR
CC active site prior to CoB for a productive catalysis.
CC {ECO:0000269|PubMed:25691570}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; X07794; CAA30639.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL59127.1; -; Genomic_DNA.
DR RefSeq; WP_013296337.1; NC_014408.1.
DR PDB; 1HBM; X-ray; 1.80 A; A/D=2-550.
DR PDB; 1HBN; X-ray; 1.16 A; A/D=2-550.
DR PDB; 1HBO; X-ray; 1.78 A; A/D=2-550.
DR PDB; 1HBU; X-ray; 1.90 A; A/D=2-550.
DR PDB; 1MRO; X-ray; 1.16 A; A/D=2-549.
DR PDB; 3M1V; X-ray; 1.45 A; A/D=2-550.
DR PDB; 3M2R; X-ray; 1.30 A; A/D=2-550.
DR PDB; 3M2U; X-ray; 1.40 A; A/D=2-550.
DR PDB; 3M2V; X-ray; 1.80 A; A/D=2-550.
DR PDB; 3M30; X-ray; 1.45 A; A/D=2-550.
DR PDB; 3M32; X-ray; 1.35 A; A/D=2-550.
DR PDB; 3POT; X-ray; 1.20 A; A/D=1-550.
DR PDB; 5A0Y; X-ray; 1.10 A; A/D=1-550.
DR PDB; 5G0R; X-ray; 1.25 A; A/D=1-550.
DR PDB; 7B2H; X-ray; 2.12 A; A/D=1-550.
DR PDB; 7SUC; X-ray; 1.90 A; A/a=2-549.
DR PDB; 7SXM; X-ray; 2.50 A; A/D=2-549.
DR PDBsum; 1HBM; -.
DR PDBsum; 1HBN; -.
DR PDBsum; 1HBO; -.
DR PDBsum; 1HBU; -.
DR PDBsum; 1MRO; -.
DR PDBsum; 3M1V; -.
DR PDBsum; 3M2R; -.
DR PDBsum; 3M2U; -.
DR PDBsum; 3M2V; -.
DR PDBsum; 3M30; -.
DR PDBsum; 3M32; -.
DR PDBsum; 3POT; -.
DR PDBsum; 5A0Y; -.
DR PDBsum; 5G0R; -.
DR PDBsum; 7B2H; -.
DR PDBsum; 7SUC; -.
DR PDBsum; 7SXM; -.
DR AlphaFoldDB; P11558; -.
DR SMR; P11558; -.
DR STRING; 79929.MTBMA_c15480; -.
DR iPTMnet; P11558; -.
DR PRIDE; P11558; -.
DR EnsemblBacteria; ADL59127; ADL59127; MTBMA_c15480.
DR GeneID; 9705257; -.
DR KEGG; mmg:MTBMA_c15480; -.
DR PATRIC; fig|79929.8.peg.1501; -.
DR HOGENOM; CLU_493170_0_0_2; -.
DR OMA; AMLYDQI; -.
DR OrthoDB; 6589at2157; -.
DR BRENDA; 2.8.4.1; 25952.
DR UniPathway; UPA00646; UER00699.
DR EvolutionaryTrace; P11558; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IDA:MENGO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.840.10; -; 1.
DR Gene3D; 3.30.70.470; -; 1.
DR Gene3D; 3.90.390.10; -; 1.
DR InterPro; IPR016212; Me_CoM_Rdtase_asu.
DR InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C.
DR InterPro; IPR009047; Me_CoM_Rdtase_asu_C.
DR InterPro; IPR003183; Me_CoM_Rdtase_asu_N.
DR InterPro; IPR015811; Me_CoM_Rdtase_asu_N_sub1.
DR InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2.
DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold.
DR Pfam; PF02249; MCR_alpha; 1.
DR Pfam; PF02745; MCR_alpha_N; 1.
DR PIRSF; PIRSF000262; MCR_alpha; 1.
DR SUPFAM; SSF48081; SSF48081; 1.
DR SUPFAM; SSF55088; SSF55088; 1.
DR TIGRFAMs; TIGR03256; met_CoM_red_alp; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Methanogenesis; Methylation; Nickel; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2269306"
FT CHAIN 2..550
FT /note="Methyl-coenzyme M reductase I subunit alpha"
FT /id="PRO_0000147456"
FT BINDING 147
FT /ligand="coenzyme F430"
FT /ligand_id="ChEBI:CHEBI:60540"
FT /ligand_part="Ni"
FT /ligand_part_id="ChEBI:CHEBI:28112"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:11491299,
FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550,
FT ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN,
FT ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V,
FT ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y,
FT ECO:0007744|PDB:5G0R"
FT BINDING 225
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /ligand_note="ligand shared between two alpha subunits"
FT /note="in chain A"
FT /evidence="ECO:0000269|PubMed:11491299,
FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550,
FT ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN,
FT ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V,
FT ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y,
FT ECO:0007744|PDB:5G0R"
FT BINDING 256..257
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /ligand_note="ligand shared between two alpha subunits"
FT /note="in chain A"
FT /evidence="ECO:0000269|PubMed:11491299,
FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550,
FT ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN,
FT ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V,
FT ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y,
FT ECO:0007744|PDB:5G0R"
FT BINDING 270
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /ligand_note="ligand shared between two alpha subunits"
FT /note="in chain B"
FT /evidence="ECO:0000269|PubMed:11491299,
FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550,
FT ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957, ECO:0007744|PDB:1HBN,
FT ECO:0007744|PDB:1MRO, ECO:0007744|PDB:3M1V,
FT ECO:0007744|PDB:3POT, ECO:0007744|PDB:5A0Y,
FT ECO:0007744|PDB:5G0R"
FT BINDING 333
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000269|PubMed:11491299,
FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550,
FT ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957,
FT ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1MRO,
FT ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT,
FT ECO:0007744|PDB:5A0Y"
FT BINDING 444
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000269|PubMed:11491299,
FT ECO:0000269|PubMed:20707311, ECO:0000269|PubMed:21438550,
FT ECO:0000269|PubMed:27467699, ECO:0000269|PubMed:9367957,
FT ECO:0007744|PDB:1HBN, ECO:0007744|PDB:1MRO,
FT ECO:0007744|PDB:3M1V, ECO:0007744|PDB:3POT,
FT ECO:0007744|PDB:5A0Y"
FT MOD_RES 257
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000269|PubMed:10660523,
FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311,
FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957"
FT MOD_RES 271
FT /note="5-methylarginine"
FT /evidence="ECO:0000269|PubMed:10660523,
FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311,
FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957"
FT MOD_RES 400
FT /note="2-methylglutamine"
FT /evidence="ECO:0000269|PubMed:10660523,
FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311,
FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957"
FT MOD_RES 445
FT /note="1-thioglycine"
FT /evidence="ECO:0000269|PubMed:10660523,
FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311,
FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957"
FT MOD_RES 450
FT /note="(Z)-2,3-didehydroaspartate"
FT /evidence="ECO:0000269|PubMed:27467699"
FT MOD_RES 452
FT /note="S-methylcysteine"
FT /evidence="ECO:0000269|PubMed:10660523,
FT ECO:0000269|PubMed:11491299, ECO:0000269|PubMed:20707311,
FT ECO:0000269|PubMed:21438550, ECO:0000269|PubMed:27467699,
FT ECO:0000269|PubMed:9367957"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:5A0Y"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 222..238
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:5A0Y"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 300..316
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:5A0Y"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 342..357
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 367..387
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 398..417
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 420..438
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 453..457
FT /evidence="ECO:0007829|PDB:5A0Y"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 485..499
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 507..512
FT /evidence="ECO:0007829|PDB:5A0Y"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:5A0Y"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:5A0Y"
SQ SEQUENCE 550 AA; 60511 MW; D55A724B6CA9EFEE CRC64;
MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK RGIPQYNPDI
GTPLGQRVLM PYQVSTTDTY VEGDDLHFVN NAAMQQMWDD IRRTVIVGLN HAHAVIEKRL
GKEVTPETIT HYLETVNHAM PGAAVVQEHM VETHPALVAD SYVKVFTGND EIADEIDPAF
VIDINKQFPE DQAETLKAEV GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK
QAAGEAATGD FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP
VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG KEYVEDKYGL
CEAPNNMDTV LDVATEVTFY GLEQYEEYPA LLEDQFGGSQ RAAVVAAAAG CSTAFATGNA
QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD QCGASNVFSI RGDEGLPLEL RGPNYPNYAM
NVGHQGEYAG ISQAPHAARG DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA
GERALITPAK
