ID   MCRX_METJA              Reviewed;         552 AA.
AC   Q60391;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=mtrA; OrderedLocusNames=MJ0083;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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; L77117; AAB98063.1; -; Genomic_DNA.
DR   PIR; C64310; C64310.
DR   RefSeq; WP_010869575.1; NC_000909.1.
DR   AlphaFoldDB; Q60391; -.
DR   SMR; Q60391; -.
DR   STRING; 243232.MJ_0083; -.
DR   PaxDb; 243232-MJ_0083; -.
DR   EnsemblBacteria; AAB98063; AAB98063; MJ_0083.
DR   GeneID; 1450922; -.
DR   KEGG; mja:MJ_0083; -.
DR   eggNOG; arCOG04857; Archaea.
DR   HOGENOM; CLU_493170_0_0_2; -.
DR   InParanoid; Q60391; -.
DR   OrthoDB; 52468at2157; -.
DR   PhylomeDB; Q60391; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000000805; 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..552
FT                   /note="Methyl-coenzyme M reductase II subunit alpha"
FT                   /id="PRO_0000147453"
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:P11558"
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:P11558"
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:P11558"
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:P11558"
FT   BINDING         335
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000250|UniProtKB:P11558"
FT   BINDING         446
FT                   /ligand="coenzyme M"
FT                   /ligand_id="ChEBI:CHEBI:58319"
FT                   /evidence="ECO:0000250|UniProtKB:P11558"
SQ   SEQUENCE   552 AA;  61241 MW;  DB66781796B987CE CRC64;
     MDVEKKLFLK ALKEKFEEDP KEKYTKFYIF GGWRQSARKR EFVEFAQKLI EKRGGIPFYN
     PDIGVPLGQR KLMTYKISGT DAFVEGDDLH FCNNAAIQQL VDDIKRTVIV GMDTAHAVLE
     KRLGVEVTPE TINEYMETIN HALPGGAVVQ EHMVEVHPGL VWDCYAKIFT GNDELADEID
     KRFLIDINKE FPEEQAEQIK KYIGNRTYQV SRVPTIVVRC CDGGTVSRWS AMQIGMSFIT
     AYKLCAGEAA IADFSYAAKH ADVIQMGMIL PARRARGPNE PGGVPFGIFA DIIQTSRVSD
     DPAQVTLEVI GAAATFYDQV WLGSYMSGGV GFTQYASATY TDDILDDFVY YGMDYVEKKY
     GLCGVKPSME VVKDIATEVT LYGLEQYDEY PALLEDHFGG SQRAGVTAAA AGCSVAFATG
     NSNAGINGWY LSQILHKEYH SRLGFYGYDL QDQCGAANSL SIRSDEGLLH ECRGPNYPNY
     AMNVGHQPEY AGIAQAPHAA RGDAFCLNPI IKVAFADDNL IFDFKWPRKC IAKGALREFE
     PAGERDLIIP AA
//