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UniProtKB/Swiss-Prot entry O27232


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MCRA_METTH
Primary accession number O27232
Secondary accession number Q50493
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 63)
Name and origin of the protein
Protein name Methyl-coenzyme M reductase subunit alpha
Synonyms EC 2.8.4.1
Coenzyme-B sulfoethylthiotransferase alpha
Gene name
Name: mcrA
OrderedLocusNames: MTH_1164
From
Methanobacterium thermoautotrophicum [TaxID: 187420] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Delta H;
PubMed=7929010 [NCBI, ExPASy, EBI, Israel, Japan]
Pihl T.D., Sharma S., Reeve J.N.;
"Growth phase-dependent transcription of the genes that encode the two methyl coenzyme M reductase isoenzymes and N5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum delta H.";
J. Bacteriol. 176:6384-6391(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Delta H;
PubMed=9371463 [NCBI, ExPASy, EBI, Israel, Japan]
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.";
J. Bacteriol. 179:7135-7155(1997).
[3]
PROTEIN SEQUENCE OF 2-19.
STRAIN=Delta H;
PubMed=2269306 [NCBI, ExPASy, EBI, Israel, Japan]
Rospert S., Linder D., Ellermann J., Thauer R.K.;
"Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H.";
Eur. J. Biochem. 194:871-877(1990).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U10036; AAA73445.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000666; AAB85653.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B69022; B69022.
RefSeq NP_276292.1; -.
3D structure databases
HSSP P11558; 1HBN. [HSSP ENTRY / PDB]
SMR O27232; 2-549.
ModBase O27232.
Enzyme and pathway databases
BioCyc MTHE187420:MTH1164-MON; -.
Ontologies
GO
GO:0016151; Molecular function: nickel ion binding (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016212; Me_Co_M_Rdtase_asu.
IPR008924; Me_CoM_Rdtase_asu/bsu_C.
IPR009047; Me_CoM_Rdtase_asu_C.
IPR003183; Me_CoM_Rdtase_asu_N.
IPR015811; Me_CoM_Rdtase_asu_N_sub1.
IPR015823; Me_CoM_Rdtase_asu_N_sub2.
Graphical view of domain structure.
Gene3D G3DSA:1.20.840.10; MCR_a/b_chain_a-bundle; 1.
G3DSA:3.90.390.10; Me_CoM_Rdtase_asu_N_sub1; 1.
G3DSA:3.30.70.470; Me_CoM_Rdtase_asu_N_sub2; 1.
Pfam PF02249; MCR_alpha; 1.
PF02745; MCR_alpha_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000262; MCR_alpha; 1.
TIGRFAMs TIGR03256; met_CoM_red_alp; 1.
BLOCKS O27232.
ProtoNet O27232.
Genome annotation databases
GeneID 1471572; -.
GenomeReviews AE000666_GR; MTH_1164.
KEGG mth:MTH1164; -.
NMPDR fig|187420.1.peg.1147; -.
Phylogenomic databases
HOGENOM O27232; -.
Genome annotation databases
CMR O27232; MTH_1164.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Metal-binding; Methanogenesis; Methylation; Nickel; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   550  549     Methyl-coenzyme M reductase subunit alpha. PRO_0000147455
METAL   147   147        Nickel (By similarity). 
MOD_RES   257   257        Pros-methylhistidine (By similarity). 
MOD_RES   270   270        5-methylarginine (By similarity). 
CONFLICT   288   288        D -> E (in Ref. 1; AAA73445). 
Sequence information
Length: 550 AA [This is the length of the unprocessed precursor] Molecular weight: 60482 Da [This is the MW of the unprocessed precursor] CRC64: DE8184A3A79468CC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK RGIPQYNPDI 

        70         80         90        100        110        120 
GTPLGQRVLM PYQVSTTDTF VEGDDLHFVN NAAMQQMWDD IRRTVIVGLN HAHAVIEKRL 

       130        140        150        160        170        180 
GKEVTPETIT HYLETVNHAM PGAAVVQEHM VETHPALVAD SYVKVFTGND EIADEIDPAF 

       190        200        210        220        230        240 
VIDINKQFPE DQAETLKAEV GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK 

       250        260        270        280        290        300 
QAAGEAATGD FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP 

       310        320        330        340        350        360 
VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG KEYVEDKYGL 

       370        380        390        400        410        420 
CEAPNTMDTV LDVASEVTFY GLEQYEEYPA LLEDQFGGSQ RAAVVAAAAG CSTAFATANA 

       430        440        450        460        470        480 
QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD QCGASNVFSI RGDEGLPLEL RGPNYPNYAM 

       490        500        510        520        530        540 
NVGHQGEYAG ISQAPHAARG DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA 

       550 
GERALITPAK 

O27232 in FASTA format

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