MCRX_METJA
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 03-AUG-2022, entry version 127.
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 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 OMA; VGHQPEY; -.
DR OrthoDB; 6589at2157; -.
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; 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 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
