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Database: UniProt
Entry: Q2NHZ8_METST
LinkDB: Q2NHZ8_METST
Original site: Q2NHZ8_METST 
ID   Q2NHZ8_METST            Unreviewed;       552 AA.
AC   Q2NHZ8;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   25-OCT-2017, entry version 71.
DE   RecName: Full=Methyl-coenzyme M reductase subunit alpha {ECO:0000256|PIRNR:PIRNR000262};
DE            EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000262};
GN   Name=mrtA {ECO:0000313|EMBL:ABC56731.1};
GN   OrderedLocusNames=Msp_0321 {ECO:0000313|EMBL:ABC56731.1};
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860 {ECO:0000313|EMBL:ABC56731.1, ECO:0000313|Proteomes:UP000001931};
RN   [1] {ECO:0000313|EMBL:ABC56731.1, ECO:0000313|Proteomes:UP000001931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3
RC   {ECO:0000313|Proteomes:UP000001931};
RX   PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H.,
RA   Hedderich R., Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this
RT   human intestinal archaeon is restricted to methanol and H2 for methane
RT   formation and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC56731.1; -; Genomic_DNA.
DR   RefSeq; WP_011405931.1; NC_007681.1.
DR   ProteinModelPortal; Q2NHZ8; -.
DR   STRING; 339860.Msp_0321; -.
DR   EnsemblBacteria; ABC56731; ABC56731; Msp_0321.
DR   GeneID; 3855926; -.
DR   KEGG; mst:Msp_0321; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   HOGENOM; HOG000225809; -.
DR   KO; K00399; -.
DR   OMA; QVWLGSY; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000001931; 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:UP000001931};
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:UP000001931};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000262,
KW   ECO:0000313|EMBL:ABC56731.1}.
FT   DOMAIN        5    271       MCR_alpha_N. {ECO:0000259|Pfam:PF02745}.
FT   DOMAIN      318    443       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   552 AA;  60333 MW;  53FA735C33CF3428 CRC64;
     MDNEKKLFLK ALKEKFDEDP EEENTKFYCY GGWEQSARKR EFAEEAEKAV EARGGLPFYN
     PDIGVPLGQR KLMAYQVSGT DTYVEGDDLH FCNNSAIQQL VDDIKRTVIV GMDTAHGVLE
     QRLGVEVTPE TINEYLETIN HALPGGAVVQ EHMVEVDPGL VTDSYAKIFT GDDDLLDQLD
     QRFVIDINKE FPEEQAEMLK KYIGKKTYQV SRVPTLVVRA CDGGTTSRWS AMQIGMSFIS
     AYKLCAGEAA IADFSYAAKH ADVISMASAM PSRRARGPNE PGGVTFGAFS DMVQTSRVTD
     DPAEVTLEVI GGAAPLYDQV WLGSYMSGGV GFTQYATAAY TDEILDDFIY YGKDYVEGKY
     GGLCQAEATS EVVKDIASEV TLYGLEQYEI PAALEDHFGG SQRAAVLAAG AGCSVAFATA
     NSNAGVNGWY LSQLLHKEGH SRLGFYGYDL QDQCGSSNSL SVRSDEGLIH ELRGPNYPNY
     AMNVGHQPEY AGIAQAPHAA RGDAFALNPL IKVAFADKNL SFDWAHPREC IAKGAVREFM
     PSGERDLINP AL
//
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