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Entry: D5VQU8_METIM
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ID   D5VQU8_METIM            Unreviewed;       553 AA.
AC   D5VQU8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   25-OCT-2017, entry version 33.
DE   RecName: Full=Methyl-coenzyme M reductase subunit alpha {ECO:0000256|PIRNR:PIRNR000262};
DE            EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000262};
GN   OrderedLocusNames=Metin_0281 {ECO:0000313|EMBL:ADG12951.1};
OS   Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG12951.1, ECO:0000313|Proteomes:UP000002061};
RN   [1] {ECO:0000313|EMBL:ADG12951.1, ECO:0000313|Proteomes:UP000002061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M.,
RA   Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanocaldococcus infernus ME.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio)
CC       ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate
CC       to methane and a heterodisulfide. {ECO:0000256|PIRNR:PIRNR000262}.
CC   -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane.
CC       {ECO:0000256|PIRNR:PIRNR000262}.
CC   -!- COFACTOR:
CC       Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000262};
CC       Note=Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme
CC       F430 is a yellow nickel porphinoid.
CC       {ECO:0000256|PIRNR:PIRNR000262};
CC   -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction;
CC       methane from methyl-coenzyme M: step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR000262}.
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains.
CC       {ECO:0000256|PIRNR:PIRNR000262}.
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DR   EMBL; CP002009; ADG12951.1; -; Genomic_DNA.
DR   RefSeq; WP_013099697.1; NC_014122.1.
DR   STRING; 573063.Metin_0281; -.
DR   EnsemblBacteria; ADG12951; ADG12951; Metin_0281.
DR   GeneID; 9131281; -.
DR   KEGG; mif:Metin_0281; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   HOGENOM; HOG000225809; -.
DR   KO; K00399; -.
DR   OMA; GRVCDGG; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000002061; Chromosome.
DR   GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-UniRule.
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   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002061};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000262,
KW   ECO:0000256|PIRSR:PIRSR000262-1};
KW   Methanogenesis {ECO:0000256|PIRNR:PIRNR000262};
KW   Nickel {ECO:0000256|PIRNR:PIRNR000262, ECO:0000256|PIRSR:PIRSR000262-
KW   1}; Reference proteome {ECO:0000313|Proteomes:UP000002061};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000262,
KW   ECO:0000313|EMBL:ADG12951.1}.
FT   DOMAIN        6    271       MCR_alpha_N. {ECO:0000259|Pfam:PF02745}.
FT   DOMAIN      318    444       MCR_alpha. {ECO:0000259|Pfam:PF02249}.
FT   METAL       150    150       Nickel. {ECO:0000256|PIRSR:PIRSR000262-
FT                                1}.
FT   MOD_RES     260    260       Pros-methylhistidine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
FT   MOD_RES     274    274       5-methylarginine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
SQ   SEQUENCE   553 AA;  61370 MW;  F1D13FD65436EA0D CRC64;
     MEAEKRLFLK ALKEKFEEDP REKYTKFYIF GGWRQSARKR EFVEAAQKLI EKRGGIPFYN
     PDIGVPLGQR KLMPYKVSNT DAIVEGDDLH FMNNAAIQQM WDDIRRTVIV GMDTAHAVLE
     KRLGVEATPE TINEYMEVIN HALPGGAVVQ EHMVEVHPAL VWDCYAKIFT GDDELADEID
     KRFLIDINKL FPEEQAEQIK KAIGKRTYQV SRVPTLVGRV CDGGTIARWS AMQIGMSFIT
     AYKLCAGEAA IADFSYAAKH ADVIQMATFL PARRARGPNE PGGMYFGVLA DVVQTTRVSD
     DPVEQSLEVV AAGAALFDQI WLGSYMSGGV GFTQYATASY TDDILDDFSY YGYDYINKKY
     GGCNSVKPTM DVVEDIATEV TLYALEQYDT YPALLEDHFG GSQRAAVTAA ASGISVALAT
     GNSNAGLNGW YLSQILHKEY HSRLGFYGYD LQDQCGAANS LSFRNDEGSP LELRGPNYPN
     YAMNVGHQGE YAGITQAAHS GRGDAFALNP LIKVAFADPS LIFDFRYPRK EFARGALREF
     EPAGERDPII PAH
//
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