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Database: UniProt
Entry: A0A150J824_9EURY
LinkDB: A0A150J824_9EURY
Original site: A0A150J824_9EURY 
ID   A0A150J824_9EURY        Unreviewed;       553 AA.
AC   A0A150J824;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 7.
DE   RecName: Full=Methyl-coenzyme M reductase subunit alpha {ECO:0000256|PIRNR:PIRNR000262};
DE            EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000262};
GN   ORFNames=AMQ22_00302 {ECO:0000313|EMBL:KYC53403.1};
OS   Arc I group archaeon U1lsi0528_Bin055.
OC   Archaea; Euryarchaeota; Methanomicrobia; unclassified Methanomicrobia;
OC   Arc I group.
OX   NCBI_TaxID=1705409 {ECO:0000313|EMBL:KYC53403.1, ECO:0000313|Proteomes:UP000075398};
RN   [1] {ECO:0000313|EMBL:KYC53403.1, ECO:0000313|Proteomes:UP000075398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U1lsi0528_Bin055 {ECO:0000313|EMBL:KYC53403.1};
RX   PubMed=26943620;
RA   Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT   "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a
RT   uniquely fastidious methyl-reducing methanogen.";
RL   ISME J. 0:0-0(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KYC53403.1}.
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DR   EMBL; LNGC01000006; KYC53403.1; -; Genomic_DNA.
DR   PATRIC; fig|1705409.3.peg.313; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000075398; Unassembled WGS sequence.
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:UP000075398};
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:UP000075398};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000262}.
FT   DOMAIN        8    272       MCR_alpha_N. {ECO:0000259|Pfam:PF02745}.
FT   DOMAIN      320    445       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   553 AA;  61221 MW;  A3DDC9767A7DA3A3 CRC64;
     MVYKDEKHNF MQAMKKKFEE APDKKNTKYY VYGGYKQNKR KVEFHDAGLQ IAKERGIPGY
     NPSVGMPQGQ RVLMPYQLSH TDIIANMDDL HFVNNAAMQQ AWDDMRRTIL VGLDSPHNIL
     EKRLGKEVTP ETINHYLEVV NHAMPGAAVI QEHMVETDPR LVKDSYVKVY SGNDELIDEI
     DSRFVIDINK EFPAAQAAEL KKAIGKSMWQ VVRIPTVVGR ICDGGTVSRW SAMQIGMAFI
     GAYNLCAGEA ATGDFAYAAK HGSVIQMSDM MPARRARGPN EPGGLMYGIV SDCAQSLAKY
     PDDPARHSLE TIALAALIYD QIYLGSYMSG GVGFTQYATA AYTDNILEDF VYWGMEHVKD
     KYGDLAKQKP SVKLINDIGT DVAMYCLEQY ELYPAVMETH FGGSQRATCI SAAAGTSVAM
     ATGNAQAGLS AWYLACNIHK EQMGRFGFYG YDLQDQIGAA NTFSYRSDEG LPFELRGGNY
     PSYAMNVGHQ SAYAGIVAAA HSSRFDAWAL SPHIKVAFAD RSLPFDFANI TKEFGRGAMR
     EFVPAGERDL IIP
//
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