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Database: UniProt
Entry: MCRX_METFV
LinkDB: MCRX_METFV
Original site: 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   28-MAR-2018, entry version 100.
DE   RecName: Full=Methyl-coenzyme M reductase II subunit alpha;
DE            Short=MCR II alpha;
DE            EC=2.8.4.1;
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 /
OS   V24 S).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   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;
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.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S.,
RA   Rohde M., Eichinger K., Huber H., Wirth R., Goker M., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Methanothermus fervidus type strain
RT   (V24S).";
RL   Stand. Genomic Sci. 3:315-324(2010).
CC   -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio)
CC       ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate
CC       to methane and a heterodisulfide. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane.
CC   -!- COFACTOR:
CC       Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme
CC       F430 is a yellow nickel porphinoid. {ECO:0000250};
CC   -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction;
CC       methane from methyl-coenzyme M: step 1/1.
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains.
CC       {ECO:0000250}.
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   SMR; Q49174; -.
DR   STRING; 523846.Mfer_0734; -.
DR   EnsemblBacteria; ADP77533; ADP77533; Mfer_0734.
DR   GeneID; 9962464; -.
DR   KEGG; mfv:Mfer_0734; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   HOGENOM; HOG000225809; -.
DR   KO; K00399; -.
DR   OMA; VGHQPEY; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   BioCyc; MFER523846:G1GOR-758-MONOMER; -.
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   Complete proteome; Metal-binding; Methanogenesis; Methylation; Nickel;
KW   Reference proteome; Transferase.
FT   CHAIN         1    554       Methyl-coenzyme M reductase II subunit
FT                                alpha.
FT                                /FTId=PRO_0000147451.
FT   METAL       151    151       Nickel. {ECO:0000250}.
FT   MOD_RES     261    261       Pros-methylhistidine. {ECO:0000250}.
FT   MOD_RES     275    275       5-methylarginine. {ECO:0000250}.
FT   CONFLICT    273    273       A -> G (in Ref. 1; CAA50044).
FT                                {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
//
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