MCRX_METTH
ID MCRX_METTH Reviewed; 553 AA.
AC P21110; O27201; Q50487;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Methyl-coenzyme M reductase II subunit alpha {ECO:0000303|PubMed:2269306};
DE Short=MCR II alpha {ECO:0000303|PubMed:2269306};
DE EC=2.8.4.1 {ECO:0000269|PubMed:2269306};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha;
GN Name=mrtA; OrderedLocusNames=MTH_1129;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=7929010; DOI=10.1128/jb.176.20.6384-6391.1994;
RA Pihl T.D., Sharma S., Reeve J.N.;
RT "Growth phase-dependent transcription of the genes that encode the two
RT methyl coenzyme M reductase isoenzymes and N5-
RT methyltetrahydromethanopterin:coenzyme M methyltransferase in
RT Methanobacterium thermoautotrophicum delta H.";
RL J. Bacteriol. 176:6384-6391(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [3]
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
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).
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 {ECO:0000269|PubMed:2269306}.
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC Evidence={ECO:0000305|PubMed:2269306};
CC -!- COFACTOR:
CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC Evidence={ECO:0000250|UniProtKB:P11558};
CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is
CC activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I)
CC oxidation state. {ECO:0000250|UniProtKB:P11558};
CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC from methyl-coenzyme M: step 1/1. {ECO:0000305|PubMed:2269306}.
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 -!- 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:0000250|UniProtKB:P11558}.
CC -!- PTM: The alpha subunit contains six modified amino acids near the
CC active site region. Is methylated on His-260, Arg-274, Gln-402 and Cys-
CC 454, probably by the action of specific S-adenosylmethionine-dependent
CC methyltransferases. Also contains a thioglycine at position 447,
CC forming a thiopeptide bond. Contains a didehydroaspartate residue at
CC position 452 (By similarity). The methylation on C5 of Arg-274 is a
CC post-translational methylation not essential in vivo, but which plays a
CC role for the stability and structural integrity of MCR (By similarity).
CC {ECO:0000250|UniProtKB:P58815, ECO:0000250|UniProtKB:Q8THH1}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; U09990; AAA73439.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85618.1; -; Genomic_DNA.
DR PIR; C69017; C69017.
DR PIR; T45150; T45150.
DR RefSeq; WP_010876753.1; NC_000916.1.
DR AlphaFoldDB; P21110; -.
DR SMR; P21110; -.
DR IntAct; P21110; 2.
DR STRING; 187420.MTH_1129; -.
DR PRIDE; P21110; -.
DR EnsemblBacteria; AAB85618; AAB85618; MTH_1129.
DR GeneID; 1471537; -.
DR KEGG; mth:MTH_1129; -.
DR PATRIC; fig|187420.15.peg.1106; -.
DR HOGENOM; CLU_493170_0_0_2; -.
DR OMA; VGHQPEY; -.
DR BioCyc; MetaCyc:MRTAMAUTO-MON; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC.
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 Direct protein sequencing; Metal-binding; Methanogenesis; Methylation;
KW Nickel; Reference proteome; Transferase.
FT CHAIN 1..553
FT /note="Methyl-coenzyme M reductase II subunit alpha"
FT /id="PRO_0000147457"
FT BINDING 150
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:0000250|UniProtKB:P58815"
FT BINDING 228
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:0000250|UniProtKB:P58815"
FT BINDING 259..260
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:0000250|UniProtKB:P58815"
FT BINDING 273
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:0000250|UniProtKB:P58815"
FT BINDING 335
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P58815"
FT BINDING 446
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P58815"
FT MOD_RES 260
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P58815"
FT MOD_RES 274
FT /note="5-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P58815"
FT MOD_RES 402
FT /note="2-methylglutamine"
FT /evidence="ECO:0000250|UniProtKB:P58815"
FT MOD_RES 447
FT /note="1-thioglycine"
FT /evidence="ECO:0000250|UniProtKB:P58815"
FT MOD_RES 452
FT /note="(Z)-2,3-didehydroaspartate"
FT /evidence="ECO:0000250|UniProtKB:P58815"
FT MOD_RES 454
FT /note="S-methylcysteine"
FT /evidence="ECO:0000250|UniProtKB:P58815"
FT CONFLICT 6
FT /note="L -> H (in Ref. 1; AAA73439)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="Y -> I (in Ref. 1; AAA73439)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="I -> V (in Ref. 1; AAA73439)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="K -> KEQLK (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 60707 MW; 8A3511715F7EFE00 CRC64;
MDEKKLFLTA LKKKFEVEDP DEKYTNFYCF GGWEQSARKK EFTEYAKKAA EKRGGIPFYN
PDIGVPLGQR KLMAYRVSGT DAYVEGDDLH FVNNAAIQQM VDDIKRTVIV GMDTAHAVLE
KRLGVEVTPE TINEYMEAIN HALPGGAVVQ EHMVEVHPGL VEDCYAKIFT GDDNLADELD
KRILIDINKE FPEEQAEQLK SYIGNRTYQV NRVPTIVVRT CDGGTVSRWS AMQIGMSFIS
AYKLCAGEAA IADFSYAAKH ADVIEMGTIM PARRARGPNE PGGVAFGTFA DIVQASRVSD
DPAKISLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY YGMEYVDDKY
GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG SQRAAVAAAA AGCSTAFATG
NSNAGINGWY LSQILHKEAH SRLGFYGYDL QDQCGASNSL SIRSDEGLIH ELRGPNYPNY
AMNVGHQPEY AGIAQAPHAA RGDAFCTNPL IKVAFADKDL SFDFTSPRKS IAAGALREFM
PEGERDLIIP AGK
