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Database: UniProt
Entry: D7DUH5_METV3
LinkDB: D7DUH5_METV3
Original site: D7DUH5_METV3 
ID   D7DUH5_METV3            Unreviewed;       554 AA.
AC   D7DUH5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   28-FEB-2018, entry version 37.
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=Mvol_1128 {ECO:0000313|EMBL:ADI36785.1};
OS   Methanococcus voltae (strain ATCC BAA-1334 / A3).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=456320 {ECO:0000313|EMBL:ADI36785.1, ECO:0000313|Proteomes:UP000007722};
RN   [1] {ECO:0000313|EMBL:ADI36785.1, ECO:0000313|Proteomes:UP000007722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1334 / A3 {ECO:0000313|Proteomes:UP000007722};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanococcus voltae A3.";
RL   Submitted (MAY-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; CP002057; ADI36785.1; -; Genomic_DNA.
DR   RefSeq; WP_013180513.1; NC_014222.1.
DR   ProteinModelPortal; D7DUH5; -.
DR   STRING; 456320.Mvol_1128; -.
DR   EnsemblBacteria; ADI36785; ADI36785; Mvol_1128.
DR   GeneID; 9276353; -.
DR   KEGG; mvo:Mvol_1128; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   HOGENOM; HOG000225809; -.
DR   KO; K00399; -.
DR   OMA; GRVCDGG; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   BioCyc; MVOL456320:G1FZ2-1127-MONOMER; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000007722; 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:UP000007722};
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:UP000007722};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000262,
KW   ECO:0000313|EMBL:ADI36785.1}.
FT   DOMAIN        6    272       MCR_alpha_N. {ECO:0000259|Pfam:PF02745}.
FT   DOMAIN      319    444       MCR_alpha. {ECO:0000259|Pfam:PF02249}.
FT   METAL       151    151       Nickel. {ECO:0000256|PIRSR:PIRSR000262-
FT                                1}.
FT   MOD_RES     261    261       Pros-methylhistidine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
FT   MOD_RES     275    275       5-methylarginine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
SQ   SEQUENCE   554 AA;  61299 MW;  FDC9E95F2851ED28 CRC64;
     MEAEKRLFLK ALKEKFEEDP KEKFTKFYTY GGWQQSERKK EFFAENERIV AEKRDGIPMY
     NPDIGVPLGQ RKLMPYKVSN TDSYVEGDDL HFMNNAAIQQ LWDDIRRTVI VGMDTAHMVL
     EKRLGVEVTP ETINEYMHTI NHSLPGGAVV QEHMVEVHPS LAWDCYAKIF TGDDELADEL
     DDRFVININK LFPEEQAEEL KAAIGKKTYQ VSRVPSLVGR VCDGGTISRW SAMQIGMSFI
     TAYKLCAGEA AIADFSYAAK HADVIQMGNA LPGRRARGPN EPGGVRFGIL SDVVQTTRVS
     DDPVEQSLEV VATGAALYDQ IWLGSYMSGG VGFTQYATAS YTDDILDDFS YYGLDYVEKK
     YGRCGTKATM DVVEDIASEV TLYALEQYDE YPALLEDHFG GSQRAAVAAA AAGISTCMAT
     GNSNAGVNGW YLSQILHKEY HSRLGFYGYD LQDQCGASNS LAIRNDEASP LELRGPNYPN
     YAMNVGHQGE YAGIAQSAHS ARGDAFATNA LIKVAFADPS LVFDFTKPRK EMARGALREF
     EAAGERDAIL PAKI
//
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