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O27232

- MCRA_METTH

UniProt

O27232 - MCRA_METTH

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Protein

Methyl-coenzyme M reductase subunit alpha

Gene
mcrA, MTH_1164
Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide.

Catalytic activityi

Methyl-CoM + CoB = CoM-S-S-CoB + methane.

Cofactori

Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme F430 is a yellow nickel porphinoid By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi147 – 1471Nickel By similarity

GO - Molecular functioni

  1. coenzyme-B sulfoethylthiotransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. methanogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

BioCyciMetaCyc:MCRAMAUTO-MONOMER.
MTHE187420:GJNM-1166-MONOMER.
UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase subunit alpha (EC:2.8.4.1)
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase alpha
Gene namesi
Name:mcrA
Ordered Locus Names:MTH_1164
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000005223: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 550549Methyl-coenzyme M reductase subunit alphaPRO_0000147455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571Pros-methylhistidine By similarity
Modified residuei271 – 27115-methylarginine By similarity

Keywords - PTMi

Methylation

Expressioni

Developmental stagei

There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I.

Interactioni

Subunit structurei

Hexamer of two alpha, two beta, and two gamma chains.

Protein-protein interaction databases

IntActiO27232. 2 interactions.
STRINGi187420.MTH1164.

Structurei

3D structure databases

ProteinModelPortaliO27232.
SMRiO27232. Positions 2-549.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG4058.
KOiK00399.
OMAiMSMISAY.

Family and domain databases

Gene3Di1.20.840.10. 1 hit.
3.30.70.470. 1 hit.
3.90.390.10. 1 hit.
InterProiIPR022681. MCR_a/b_chain_a-bundle.
IPR016212. Me_CoM_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.
IPR009024. Me_CoM_Rdtase_Fd-like_fold.
[Graphical view]
PfamiPF02249. MCR_alpha. 1 hit.
PF02745. MCR_alpha_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000262. MCR_alpha. 1 hit.
SUPFAMiSSF48081. SSF48081. 1 hit.
SSF55088. SSF55088. 1 hit.
TIGRFAMsiTIGR03256. met_CoM_red_alp. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O27232-1 [UniParc]FASTAAdd to Basket

« Hide

MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK    50
RGIPQYNPDI GTPLGQRVLM PYQVSTTDTF VEGDDLHFVN NAAMQQMWDD 100
IRRTVIVGLN HAHAVIEKRL GKEVTPETIT HYLETVNHAM PGAAVVQEHM 150
VETHPALVAD SYVKVFTGND EIADEIDPAF VIDINKQFPE DQAETLKAEV 200
GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK QAAGEAATGD 250
FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP 300
VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG 350
KEYVEDKYGL CEAPNTMDTV LDVASEVTFY GLEQYEEYPA LLEDQFGGSQ 400
RAAVVAAAAG CSTAFATANA QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD 450
QCGASNVFSI RGDEGLPLEL RGPNYPNYAM NVGHQGEYAG ISQAPHAARG 500
DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA GERALITPAK 550
Length:550
Mass (Da):60,482
Last modified:January 23, 2007 - v3
Checksum:iDE8184A3A79468CC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti288 – 2881D → E in AAA73445. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U10036 Genomic DNA. Translation: AAA73445.1.
AE000666 Genomic DNA. Translation: AAB85653.1.
PIRiB69022.
RefSeqiNP_276292.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85653; AAB85653; MTH_1164.
GeneIDi1471572.
KEGGimth:MTH1164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U10036 Genomic DNA. Translation: AAA73445.1 .
AE000666 Genomic DNA. Translation: AAB85653.1 .
PIRi B69022.
RefSeqi NP_276292.1. NC_000916.1.

3D structure databases

ProteinModelPortali O27232.
SMRi O27232. Positions 2-549.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O27232. 2 interactions.
STRINGi 187420.MTH1164.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB85653 ; AAB85653 ; MTH_1164 .
GeneIDi 1471572.
KEGGi mth:MTH1164.

Phylogenomic databases

eggNOGi COG4058.
KOi K00399.
OMAi MSMISAY.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .
BioCyci MetaCyc:MCRAMAUTO-MONOMER.
MTHE187420:GJNM-1166-MONOMER.

Family and domain databases

Gene3Di 1.20.840.10. 1 hit.
3.30.70.470. 1 hit.
3.90.390.10. 1 hit.
InterProi IPR022681. MCR_a/b_chain_a-bundle.
IPR016212. Me_CoM_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.
IPR009024. Me_CoM_Rdtase_Fd-like_fold.
[Graphical view ]
Pfami PF02249. MCR_alpha. 1 hit.
PF02745. MCR_alpha_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000262. MCR_alpha. 1 hit.
SUPFAMi SSF48081. SSF48081. 1 hit.
SSF55088. SSF55088. 1 hit.
TIGRFAMsi TIGR03256. met_CoM_red_alp. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Pihl T.D., Sharma S., Reeve J.N.
    J. Bacteriol. 176:6384-6391(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  3. "Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H."
    Rospert S., Linder D., Ellermann J., Thauer R.K.
    Eur. J. Biochem. 194:871-877(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Entry informationi

Entry nameiMCRA_METTH
AccessioniPrimary (citable) accession number: O27232
Secondary accession number(s): Q50493
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

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