MCRA_METJA
ID MCRA_METJA Reviewed; 553 AA.
AC Q58256; Q977G8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Methyl-coenzyme M reductase I subunit alpha;
DE Short=MCR I alpha;
DE EC=2.8.4.1 {ECO:0000250|UniProtKB:P11558};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha;
GN Name=mcrA; OrderedLocusNames=MJ0846;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-478.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=12427943; DOI=10.1099/00221287-148-11-3521;
RA Luton P.E., Wayne J.M., Sharp R.J., Riley P.W.;
RT "The mcrA gene as an alternative to 16S rRNA in the phylogenetic analysis
RT of methanogen populations in landfill.";
RL Microbiology 148:3521-3530(2002).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11558}.
CC -!- PTM: Is methylated on C5 of Arg-274 by the methyltransferase MJ0841.
CC This post-translational methylation, despite being not essential in
CC vivo, plays a role for the stability and structural integrity of MCR.
CC {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; L77117; AAB98851.1; -; Genomic_DNA.
DR EMBL; AF414040; AAL29289.1; -; Genomic_DNA.
DR RefSeq; WP_010870360.1; NC_000909.1.
DR PDB; 6PEU; X-ray; 1.95 A; M/N/P/Q=442-453.
DR PDBsum; 6PEU; -.
DR AlphaFoldDB; Q58256; -.
DR SMR; Q58256; -.
DR STRING; 243232.MJ_0846; -.
DR PRIDE; Q58256; -.
DR EnsemblBacteria; AAB98851; AAB98851; MJ_0846.
DR GeneID; 1451734; -.
DR KEGG; mja:MJ_0846; -.
DR eggNOG; arCOG04857; Archaea.
DR HOGENOM; CLU_493170_0_0_2; -.
DR InParanoid; Q58256; -.
DR OMA; AMLYDQI; -.
DR OrthoDB; 6589at2157; -.
DR PhylomeDB; Q58256; -.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 3D-structure; Cytoplasm; Metal-binding; Methanogenesis; Methylation;
KW Nickel; Reference proteome; Transferase.
FT CHAIN 1..553
FT /note="Methyl-coenzyme M reductase I subunit alpha"
FT /id="PRO_0000147452"
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 447
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P11558"
FT MOD_RES 274
FT /note="5-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8THH1"
FT CONFLICT 424
FT /note="N -> F (in Ref. 2; AAL29289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 61266 MW; CC3AB9AC4F745A24 CRC64;
MDAEKRLFLK ALKEKFEEDP REKYTKFYVF GGWRQSARKR EFVEAAQKLI EKRGGIPFYN
PDIGVPLGQR KLMPYKVSNT DAIVEGDDLH FMNNAAMQQF WDDIRRTVIV GMDTAHAVLE
KRLGVEVTPE TINEYMETIN HALPGGAVVQ EHMVEVHPAL VWDCYAKIFT GDDELADEID
KRFLIDINKL FPEEQAEQIK KAIGKRTYQV SRVPTLVGRV CDGGTIARWS AMQIGMSFIT
AYKLCAGEAA IADFSYAAKH ADVIQMASFL PARRARGPNE PGGIFFGVLA DIVQTSRVSD
DPVEQSLEVV AAGAMLYDQI WLGGYMSGGV GFTQYATATY TDDILDDFSY YGYDYITKKY
GGCNSVKPTM DVVEDIATEV TLYGLEQYDT FPALLEDHFG GSQRAGVTAA AAGITTALAT
GNSNAGVNGW YLSQILHKEY HSRLGFYGYD LQDQCGAANS LSFRNDEGSP LELRGPNYPN
YAMNVGHQGE YAGITQAAHS ARGDAFALNP LIKVAFADPS LVFDFTHPRK EFARGALREF
EPAGERDPII PAH
