ID   MCRA_METTH              Reviewed;         550 AA.
AC   O27232; Q50493;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 68.
DE   RecName: Full=Methyl-coenzyme M reductase subunit alpha;
DE            EC=2.8.4.1;
DE   AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha;
GN   Name=mcrA; OrderedLocusNames=MTH_1164;
OS   Methanobacterium thermoautotrophicum.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Delta H;
RX   MEDLINE=95014084; PubMed=7929010;
RA   Pihl T.D., Sharma S., Reeve J.N.;
RT   "Growth phase-dependent transcription of the genes that encode the two
RT   methyl coenzyme M reductase isoenzymes and N5-
RT   methyltetrahydromethanopterin:coenzyme M methyltransferase in
RT   Methanobacterium thermoautotrophicum delta H.";
RL   J. Bacteriol. 176:6384-6391(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Delta H;
RX   MEDLINE=98037514; PubMed=9371463;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-19.
RC   STRAIN=Delta H;
RX   MEDLINE=91099370; PubMed=2269306;
RX   DOI=10.1111/j.1432-1033.1990.tb19481.x;
RA   Rospert S., Linder D., Ellermann J., Thauer R.K.;
RT   "Two genetically distinct methyl-coenzyme M reductases in
RT   Methanobacterium thermoautotrophicum strain Marburg and delta H.";
RL   Eur. J. Biochem. 194:871-877(1990).
CC   -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio)
CC       ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate
CC       to methane and an heterodisulfide.
CC   -!- CATALYTIC ACTIVITY: 2-(methylthio)ethanesulfonate (methyl-CoM) +
CC       N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = CoM-
CC       S-S-CoB + methane.
CC   -!- COFACTOR: Binds 2 coenzyme F430 noncovalently per hexamer.
CC       Coenzyme F430 is a yellow nickel porphinoid (By similarity).
CC   -!- PATHWAY: One-carbon metabolism; methyl-CoM reduction; methane from
CC       methyl-CoM: step 1/1.
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains.
CC   -!- DEVELOPMENTAL STAGE: There are two MCR complexes in this bacteria.
CC       MCR II is expressed in the early growth phase. Late growth cells
CC       contains mostly MCR I.
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DR   EMBL; U10036; AAA73445.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB85653.1; -; Genomic_DNA.
DR   PIR; B69022; B69022.
DR   RefSeq; NP_276292.1; -.
DR   HSSP; P11558; 1HBN.
DR   SMR; O27232; 2-549.
DR   GeneID; 1471572; -.
DR   GenomeReviews; AE000666_GR; MTH_1164.
DR   KEGG; mth:MTH1164; -.
DR   NMPDR; fig|187420.1.peg.1147; -.
DR   HOGENOM; O27232; -.
DR   OMA; O27232; MSMISAY.
DR   BioCyc; MTHE187420:MTH1164-MON; -.
DR   BRENDA; 2.8.4.1; 270.
DR   GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:EC.
DR   GO; GO:0016151; F:nickel ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
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   Gene3D; G3DSA:1.20.840.10; MCR_a/b_chain_a-bundle; 1.
DR   Gene3D; G3DSA:3.90.390.10; Me_CoM_Rdtase_asu_N_sub1; 1.
DR   Gene3D; G3DSA:3.30.70.470; Me_CoM_Rdtase_asu_N_sub2; 1.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
DR   PIRSF; PIRSF000262; MCR_alpha; 1.
DR   TIGRFAMs; TIGR03256; met_CoM_red_alp; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Metal-binding;
KW   Methanogenesis; Methylation; Nickel; Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    550       Methyl-coenzyme M reductase subunit
FT                                alpha.
FT                                /FTId=PRO_0000147455.
FT   METAL       147    147       Nickel (By similarity).
FT   MOD_RES     257    257       Pros-methylhistidine (By similarity).
FT   MOD_RES     270    270       5-methylarginine (By similarity).
FT   CONFLICT    288    288       D -> E (in Ref. 1; AAA73445).
SQ   SEQUENCE   550 AA;  60482 MW;  DE8184A3A79468CC CRC64;
     MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK RGIPQYNPDI
     GTPLGQRVLM PYQVSTTDTF VEGDDLHFVN NAAMQQMWDD IRRTVIVGLN HAHAVIEKRL
     GKEVTPETIT HYLETVNHAM PGAAVVQEHM VETHPALVAD SYVKVFTGND EIADEIDPAF
     VIDINKQFPE DQAETLKAEV GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK
     QAAGEAATGD FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP
     VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG KEYVEDKYGL
     CEAPNTMDTV LDVASEVTFY GLEQYEEYPA LLEDQFGGSQ RAAVVAAAAG CSTAFATANA
     QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD QCGASNVFSI RGDEGLPLEL RGPNYPNYAM
     NVGHQGEYAG ISQAPHAARG DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA
     GERALITPAK
//