MCRA_METAC
ID MCRA_METAC Reviewed; 570 AA.
AC Q8THH1;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Methyl-coenzyme M reductase subunit alpha;
DE EC=2.8.4.1 {ECO:0000250|UniProtKB:P11558};
DE AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha;
GN Name=mcrA; OrderedLocusNames=MA_4546 {ECO:0000312|EMBL:AAM07885.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP METHYLATION AT ARG-285 BY MA_4551.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=29743535; DOI=10.1038/s41598-018-25716-x;
RA Deobald D., Adrian L., Schoene C., Rother M., Layer G.;
RT "Identification of a unique radical SAM methyltransferase required for the
RT sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase.";
RL Sci. Rep. 8:7404-7404(2018).
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:P07962};
CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC F430 is a yellow nickel porphinoid (By similarity). 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:P07962, 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:P07962}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11558}.
CC -!- PTM: Is methylated on C5 of Arg-285 by the methyltransferase MA_4551.
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:0000269|PubMed:29743535}.
CC -!- SIMILARITY: Belongs to the methyl-coenzyme M reductase alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; AE010299; AAM07885.1; -; Genomic_DNA.
DR RefSeq; WP_011024419.1; NC_003552.1.
DR AlphaFoldDB; Q8THH1; -.
DR SMR; Q8THH1; -.
DR STRING; 188937.MA_4546; -.
DR iPTMnet; Q8THH1; -.
DR EnsemblBacteria; AAM07885; AAM07885; MA_4546.
DR GeneID; 1476440; -.
DR KEGG; mac:MA_4546; -.
DR HOGENOM; CLU_493170_0_0_2; -.
DR InParanoid; Q8THH1; -.
DR OMA; AMLYDQI; -.
DR OrthoDB; 6589at2157; -.
DR PhylomeDB; Q8THH1; -.
DR BRENDA; 2.8.4.1; 7224.
DR UniPathway; UPA00646; UER00699.
DR Proteomes; UP000002487; 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 Cytoplasm; Metal-binding; Methanogenesis; Methylation; Nickel;
KW Reference proteome; Transferase.
FT CHAIN 1..570
FT /note="Methyl-coenzyme M reductase subunit alpha"
FT /id="PRO_0000446662"
FT BINDING 161
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:P07962"
FT BINDING 239
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:P07962"
FT BINDING 270..271
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:P07962"
FT BINDING 284
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:P07962"
FT BINDING 346
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P07962"
FT BINDING 464
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000250|UniProtKB:P07962"
FT MOD_RES 285
FT /note="5-methylarginine"
FT /evidence="ECO:0000269|PubMed:29743535"
SQ SEQUENCE 570 AA; 62075 MW; D7B7CCD2899E48D3 CRC64;
MAADIFAKFK KSMEVKFTQE YGSNKQAGGD ITGKTEKFLR LGPEQDARKQ EMIKAGKEIA
EKRGIAFYNP MMHMGAPLGQ RAITPYTISG TDIVAEPDDL HYVNNAAMQQ MWDDIRRTCI
VGLDMAHETL EKRLGKEVTP ETINHYLETL NHAMPGAAVV QEMMVETHPA LVDDCYVKIF
TGDDELADEI DKQYVINVNK MFSEEQAAQI KASIGKTTWQ AIHIPTIVSR TTDGAQTSRW
AAMQIGMSFI SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL
SDIVQTSRVS KDPAKIALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA YTDDILDNNT
YYDVDYINDK YNGAANLGTD NKVKATLDVV KDIATESTLY GIETYEKFPT ALEDHFGGSQ
RATVLAAASG VACALATGNA NAGLSGWYLS MYVHKEAWGR LGFFGFDLQD QCGATNVLSY
QGDEGLPDEL RGPNYPNYAM NVGHQGGYAG IAQAAHSGRG DAFTVNPLLK VCFADELMPF
NFAEPRREFG RGAIREFMPA GERSLVIPAK
