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P58815

- MCRX_METTM

UniProt

P58815 - MCRX_METTM

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Protein

Methyl-coenzyme M reductase II subunit alpha

Gene
mrtA, MTBMA_c15120
Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 3 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi150 – 1501Nickel 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

BioCyciMMAR79929:GH5J-1516-MONOMER.
UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase II subunit alpha (EC:2.8.4.1)
Short name:
MCR II alpha
Gene namesi
Name:mrtA
Ordered Locus Names:MTBMA_c15120
OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000000345: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Methyl-coenzyme M reductase II subunit alphaPRO_0000147458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601Pros-methylhistidine By similarity
Modified residuei274 – 27415-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.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000225809.
KOiK00399.
OMAiGHQPEYA.

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.

P58815-1 [UniParc]FASTAAdd to Basket

« Hide

MDEKKLFLKA LKKKFEGEDP DEKYTNFYCF GGWEQSARKK EFTEYAKKAA    50
EKRGGIPFYN PDIGVPLGQR KLMAYRVSGT DAYVEGDDLH FVNNAAIQQM 100
VDDIKRTVIV GMDTAHAVLE KRLGVEVTPE TINEYMEAIN HALPGGAVVQ 150
EHMVEVHPGL VEDCYAKIFT GDDNLADELD KRILIDINKE FPEEQAEQLK 200
SYIGNRTYQV NRVPTIVVRT CDGGTVSRWS AMQIGMSFIS AYKLCAGEAA 250
IADFSYAAKH ADVIEMGTIM PARRARGPNE PGGVAFGTFA DIVQTSRVSD 300
DPANVSLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY 350
YGMEYVDDKY GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG 400
SQRAAVAAAA AGCSTAFATG NSNAGINGWY LSQILHKEAH SRLGFYGYDL 450
QDQCGASNSL SIRSDEGLIH ELRGPNYPNY AMNVGHQPEY AGIAQAPHAA 500
RGDAFCTNPL IKVAFADKDL AFDFTSPRKS IAAGALREFM PEGERDLIIP 550
AGK 553
Length:553
Mass (Da):60,678
Last modified:November 30, 2010 - v2
Checksum:i94CC0D641E7C8271
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21D → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001710 Genomic DNA. Translation: ADL59091.1.
RefSeqiYP_003850404.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL59091; ADL59091; MTBMA_c15120.
GeneIDi9705221.
KEGGimmg:MTBMA_c15120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001710 Genomic DNA. Translation: ADL59091.1 .
RefSeqi YP_003850404.1. NC_014408.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADL59091 ; ADL59091 ; MTBMA_c15120 .
GeneIDi 9705221.
KEGGi mmg:MTBMA_c15120.

Phylogenomic databases

HOGENOMi HOG000225809.
KOi K00399.
OMAi GHQPEYA.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .
BioCyci MMAR79929:GH5J-1516-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. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
    Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
    J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  2. "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 1-14.
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Entry informationi

Entry nameiMCRX_METTM
AccessioniPrimary (citable) accession number: P58815
Secondary accession number(s): D9PXZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: November 30, 2010
Last modified: September 3, 2014
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

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