ID   MCRX_METFV              Reviewed;         554 AA.
AC   Q49174; E3GZ01;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Methyl-coenzyme M reductase II subunit alpha;
DE            Short=MCR II alpha;
DE            EC=2.8.4.1 {ECO:0000250|UniProtKB:P11558};
DE   AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha;
GN   Name=mrtA; Synonyms=mcrIIA; OrderedLocusNames=Mfer_0734;
OS   Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=523846;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX   PubMed=8177216; DOI=10.1007/bf00280317;
RA   Lehmacher A., Klenk H.-P.;
RT   "Characterization and phylogeny of mcrII, a gene cluster encoding an
RT   isoenzyme of methyl coenzyme M reductase from hyperthermophilic
RT   Methanothermus fervidus.";
RL   Mol. Gen. Genet. 243:198-206(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX   PubMed=21304736; DOI=10.4056/sigs.1283367;
RA   Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA   Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA   Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL   Stand. Genomic Sci. 3:315-324(2010).
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:0000250|UniProtKB:P11558}.
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:0000250|UniProtKB:P11558};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533;
CC         Evidence={ECO:0000250|UniProtKB:P11558};
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:0000250|UniProtKB:P11558}.
CC   -!- SUBUNIT: MCR is a hexamer of two alpha, two beta, and two gamma chains,
CC       forming a dimer of heterotrimers. {ECO:0000250|UniProtKB:P11558}.
CC   -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit
CC       family. {ECO:0000305}.
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DR   EMBL; X70765; CAA50044.1; -; Genomic_DNA.
DR   EMBL; CP002278; ADP77533.1; -; Genomic_DNA.
DR   PIR; S43897; S43897.
DR   RefSeq; WP_013413811.1; NC_014658.1.
DR   AlphaFoldDB; Q49174; -.
DR   SMR; Q49174; -.
DR   STRING; 523846.Mfer_0734; -.
DR   GeneID; 9962464; -.
DR   KEGG; mfv:Mfer_0734; -.
DR   HOGENOM; CLU_493170_0_0_2; -.
DR   OrthoDB; 52468at2157; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000002315; 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   3: Inferred from homology;
KW   Metal-binding; Methanogenesis; Methylation; Nickel; Reference proteome;
KW   Transferase.
FT   CHAIN           1..554
FT                   /note="Methyl-coenzyme M reductase II subunit alpha"
FT                   /id="PRO_0000147451"
FT   BINDING         151
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:P11558"
FT   BINDING         229
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:P11558"
FT   BINDING         260..261
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:P11558"
FT   BINDING         274
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:P11558"
FT   BINDING         336
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000250|UniProtKB:P11558"
FT   BINDING         447
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000250|UniProtKB:P11558"
FT   CONFLICT        273
FT                   /note="A -> G (in Ref. 1; CAA50044)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   554 AA;  61326 MW;  E894701807E22919 CRC64;
     MNKKNKKLFL EALEKKFKGE SPEEKKTTFY CFGGWKQSER KREFVEYAKK LAKKRGIPFY
     NPDIGVPLGQ RKLMAYRISG TDAYVEGDDL HFVNNAAIQQ MVDDIKRTVI VGMDTAHAVL
     EKRLGVEVTP ETINEYMETI NHALPGGAVV QEHMVEVHPG LVDDCYAKIF TGNDELADEL
     DKRVLIDINK EFPEEQAEML KKYIGNRTYQ VNRVPTIVVR CCDGGTVSRW SAMQIGMSFI
     SAYKLCAGEA AIADFSFAAK HADVIEMGTI LPARRARGPN EPGGIPFGVF ADIIQTSRVS
     DDPARISLEV IGAAATLYDQ VWLGSYMSGG VGFTQYASAT YTDDILDDFV YYGAEYVEDK
     YGFCGVKPSM EVVKDIATEV TLYGLEQYEE YPTLLEDHFG GSQRAAVVAA AAGCSTAFAT
     GNSNAGINAW YLSQILHKEG HSRLGFYGYD LQDQCGASNS LSIRSDEGLV HELRGPNYPN
     YAMNVGHQPE YAGIAQAPHA ARGDAFVVNP LIKVAFADND LSFDFRWPRK EIARGALREF
     MPDGERTLII PASK
//