MCRA_METKA
ID MCRA_METKA Reviewed; 553 AA.
AC Q49605;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, 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=MK0655;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8863453; DOI=10.1099/00207713-46-4-1170;
RA Noelling J., Elfner A., Palmer J.R., Steigerwald V.J., Pihl T.D.,
RA Lake J.A., Reeve J.N.;
RT "Phylogeny of Methanopyrus kandleri based on methyl coenzyme M reductase
RT operons.";
RL Int. J. Syst. Bacteriol. 46:1170-1173(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN [3] {ECO:0007744|PDB:1E6V}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH COENZYME F430;
RP COENZYME B; COENZYME M AND MCR SUBUNITS BETA AND GAMMA, FUNCTION, COFACTOR,
RP AND SUBUNIT.
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11023796; DOI=10.1006/jmbi.2000.4136;
RA Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.;
RT "Comparison of three methyl-coenzyme M reductases from phylogenetically
RT distant organisms: unusual amino acid modification, conservation and
RT adaptation.";
RL J. Mol. Biol. 303:329-344(2000).
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:0000305|PubMed:11023796}.
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:0000269|PubMed:11023796};
CC Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC F430 is a yellow nickel porphinoid (PubMed:11023796). 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:P11558, ECO:0000269|PubMed:11023796};
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:0000269|PubMed:11023796}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; U57340; AAB02003.1; -; Genomic_DNA.
DR EMBL; AE009439; AAM01870.1; -; Genomic_DNA.
DR PDB; 1E6V; X-ray; 2.70 A; A/D=1-553.
DR PDBsum; 1E6V; -.
DR AlphaFoldDB; Q49605; -.
DR SMR; Q49605; -.
DR STRING; 190192.MK0655; -.
DR PRIDE; Q49605; -.
DR EnsemblBacteria; AAM01870; AAM01870; MK0655.
DR KEGG; mka:MK0655; -.
DR PATRIC; fig|190192.8.peg.694; -.
DR HOGENOM; CLU_493170_0_0_2; -.
DR OMA; AMLYDQI; -.
DR BRENDA; 2.8.4.1; 3274.
DR UniPathway; UPA00646; UER00699.
DR EvolutionaryTrace; Q49605; -.
DR Proteomes; UP000001826; 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_0000147454"
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:0000269|PubMed:11023796,
FT ECO:0007744|PDB:1E6V"
FT BINDING 259
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000269|PubMed:11023796,
FT ECO:0007744|PDB:1E6V"
FT BINDING 273
FT /ligand="coenzyme B"
FT /ligand_id="ChEBI:CHEBI:58596"
FT /evidence="ECO:0000269|PubMed:11023796,
FT ECO:0007744|PDB:1E6V"
FT BINDING 336
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000269|PubMed:11023796,
FT ECO:0007744|PDB:1E6V"
FT BINDING 447
FT /ligand="coenzyme M"
FT /ligand_id="ChEBI:CHEBI:58319"
FT /evidence="ECO:0000269|PubMed:11023796,
FT ECO:0007744|PDB:1E6V"
FT CONFLICT 90
FT /note="H -> T (in Ref. 1; AAB02003)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="T -> P (in Ref. 1; AAB02003)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="H -> Q (in Ref. 1; AAB02003)"
FT /evidence="ECO:0000305"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:1E6V"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1E6V"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:1E6V"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:1E6V"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1E6V"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1E6V"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:1E6V"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 223..242
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:1E6V"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 303..319
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 345..360
FT /evidence="ECO:0007829|PDB:1E6V"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 370..390
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 401..420
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 423..441
FT /evidence="ECO:0007829|PDB:1E6V"
FT TURN 447..450
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 451..461
FT /evidence="ECO:0007829|PDB:1E6V"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:1E6V"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 488..502
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:1E6V"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 528..536
FT /evidence="ECO:0007829|PDB:1E6V"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:1E6V"
SQ SEQUENCE 553 AA; 61384 MW; F26582E0DCF2A434 CRC64;
MSSAEEKLFM KALKEKFEES PEEKYTKFYI FGGWKQSERK KEFKEWADKI VEERGVPHYN
PDIGVPLGQR KLMSYQVSGT DVFVEGDDLH FVNNAAMQQM WDDIRRTVIV GMDTAHRVLE
RRLGKEVTPE TINEYMETLN HALPGGAVVQ EHMVEIHPGL TWDCYAKIIT GDLELADEID
DKFLIDIEKL FPEEQAEQLI KAIGNRTYQV CRMPTIVGHV CDGATMYRWA AMQIAMSFIC
AYKIAAGEAA VSDFAFASKH AEVINMGEML PARRARGENE PGGVPFGVLA DCVQTMRKYP
DDPAKVALEV IAAGAMLYDQ IWLGSYMSGG VGFTQYATAV YTDNILDDYV YYGLEYVEDK
YGIAEAEPSM DVVKDVATEV TLYGLEQYER YPAAMETHFG GSQRAAVCAA AAGCSTAFAT
GHAQAGLNGW YLSQILHKEG HGRLGFYGYA LQDQCGAANS LSVRSDEGLP LELRGPNYPN
YAMNVGHLGE YAGIVQAAHA ARGDAFCVHP VIKVAFADEN LVFDFTEPRK EFAKGALREF
EPAGERDLIV PAE
