ID   MCRX_METTM              Reviewed;         553 AA.
AC   P58815; D9PXZ3;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   27-MAR-2024, entry version 85.
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};
GN   Name=mrtA; OrderedLocusNames=MTBMA_c15120;
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 [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   [2]
RP   PROTEIN SEQUENCE OF 1-14, 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   [3] {ECO:0007744|PDB:5A8R}
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH COENZYME F430;
RP   COENZYME B; COENZYME M AND MCR SUBUNITS BETA AND GAMMA, COFACTOR,
RP   METHYLATION AT HIS-260; ARG-274; GLN-402 AND CYS-454, THIOCARBOXYLATION AT
RP   GLY-447, DEHYDROGENATION AT ASP-452, AND SUBUNIT.
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).
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:0000269|PubMed:27467699};
CC       Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC       F430 is a yellow nickel porphinoid (PubMed:27467699). Methyl-coenzyme-M
CC       reductase is activated when the enzyme-bound coenzyme F430 is reduced
CC       to the Ni(I) oxidation state (By similarity).
CC       {ECO:0000250|UniProtKB:P11558, ECO:0000269|PubMed:27467699};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=75 uM for coenzyme B {ECO:0000269|PubMed:2269306};
CC         KM=4 mM for methyl-coenzyme M {ECO:0000269|PubMed:2269306};
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:0000269|PubMed:2269306,
CC       ECO:0000269|PubMed:27467699}.
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 (PubMed:27467699). 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:Q8THH1, ECO:0000269|PubMed:27467699}.
CC   -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001710; ADL59091.1; -; Genomic_DNA.
DR   RefSeq; WP_013296302.1; NC_014408.1.
DR   PDB; 5A8R; X-ray; 2.15 A; A/D/G/J=1-553.
DR   PDBsum; 5A8R; -.
DR   AlphaFoldDB; P58815; -.
DR   SMR; P58815; -.
DR   STRING; 79929.MTBMA_c15120; -.
DR   iPTMnet; P58815; -.
DR   PaxDb; 79929-MTBMA_c15120; -.
DR   GeneID; 9705221; -.
DR   KEGG; mmg:MTBMA_c15120; -.
DR   PATRIC; fig|79929.8.peg.1465; -.
DR   HOGENOM; CLU_493170_0_0_2; -.
DR   OrthoDB; 52468at2157; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000000345; 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; 3.30.70.470; -; 1.
DR   Gene3D; 1.20.840.10; Methyl-coenzyme M reductase, alpha/beta subunit, C-terminal; 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   NCBIfam; TIGR03256; met_CoM_red_alp; 1.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
DR   PIRSF; PIRSF000262; MCR_alpha; 1.
DR   SUPFAM; SSF48081; Methyl-coenzyme M reductase alpha and beta chain C-terminal domain; 1.
DR   SUPFAM; SSF55088; Methyl-coenzyme M reductase subunits; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Metal-binding; Methanogenesis;
KW   Methylation; Nickel; Transferase.
FT   CHAIN           1..553
FT                   /note="Methyl-coenzyme M reductase II subunit alpha"
FT                   /id="PRO_0000147458"
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:0000269|PubMed:27467699,
FT                   ECO:0007744|PDB:5A8R"
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:0000269|PubMed:27467699,
FT                   ECO:0007744|PDB:5A8R"
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:0000269|PubMed:27467699,
FT                   ECO:0007744|PDB:5A8R"
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:0000269|PubMed:27467699,
FT                   ECO:0007744|PDB:5A8R"
FT   BINDING         335
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000269|PubMed:27467699,
FT                   ECO:0007744|PDB:5A8R"
FT   BINDING         446
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000269|PubMed:27467699,
FT                   ECO:0007744|PDB:5A8R"
FT   MOD_RES         260
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000269|PubMed:27467699"
FT   MOD_RES         274
FT                   /note="5-methylarginine"
FT                   /evidence="ECO:0000269|PubMed:27467699"
FT   MOD_RES         402
FT                   /note="2-methylglutamine"
FT                   /evidence="ECO:0000269|PubMed:27467699"
FT   MOD_RES         447
FT                   /note="1-thioglycine"
FT                   /evidence="ECO:0000269|PubMed:27467699"
FT   MOD_RES         452
FT                   /note="(Z)-2,3-didehydroaspartate"
FT                   /evidence="ECO:0000269|PubMed:27467699"
FT   MOD_RES         454
FT                   /note="S-methylcysteine"
FT                   /evidence="ECO:0000269|PubMed:27467699"
FT   CONFLICT        2
FT                   /note="D -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           8..14
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           37..48
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   TURN            49..55
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           95..105
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          107..112
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           113..121
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           129..142
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          165..171
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           173..178
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           181..183
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           187..190
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           193..203
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          207..212
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           215..220
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           225..241
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           251..259
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   TURN            260..262
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          278..280
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           286..292
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           295..297
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           302..317
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           318..325
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           333..337
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   TURN            338..340
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           344..359
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           369..389
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           391..396
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           400..419
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           422..440
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           455..459
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   TURN            464..466
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           470..472
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           478..480
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          484..486
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           487..501
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           509..514
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   STRAND          520..522
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           527..535
FT                   /evidence="ECO:0007829|PDB:5A8R"
FT   HELIX           546..548
FT                   /evidence="ECO:0007829|PDB:5A8R"
SQ   SEQUENCE   553 AA;  60678 MW;  94CC0D641E7C8271 CRC64;
     MDEKKLFLKA LKKKFEGEDP 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 DIVQTSRVSD
     DPANVSLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY YGMEYVDDKY
     GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG SQRAAVAAAA AGCSTAFATG
     NSNAGINGWY LSQILHKEAH SRLGFYGYDL QDQCGASNSL SIRSDEGLIH ELRGPNYPNY
     AMNVGHQPEY AGIAQAPHAA RGDAFCTNPL IKVAFADKDL AFDFTSPRKS IAAGALREFM
     PEGERDLIIP AGK
//