MCRX_METFV
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 03-AUG-2022, entry version 111.
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 EnsemblBacteria; ADP77533; ADP77533; Mfer_0734.
DR GeneID; 9962464; -.
DR KEGG; mfv:Mfer_0734; -.
DR HOGENOM; CLU_493170_0_0_2; -.
DR OMA; VGHQPEY; -.
DR OrthoDB; 6589at2157; -.
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; 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..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
