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Protein

Methyl-coenzyme M reductase II subunit alpha

Gene

mrtA

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: 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

coenzyme F430Note: Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme F430 is a yellow nickel porphinoid.

Pathway: methyl-coenzyme M reduction

This protein is involved in step 1 of the subpathway that synthesizes methane from methyl-coenzyme M.
Proteins known to be involved in this subpathway in this organism are:
  1. Methyl-coenzyme M reductase II subunit alpha (mrtA), Methyl-coenzyme M reductase I subunit beta (mcrB), Methyl-coenzyme M reductase II subunit gamma (mrtG), Methyl-coenzyme M reductase I subunit alpha (mcrA), Methyl-coenzyme M reductase I subunit gamma (mcrG)
This subpathway is part of the pathway methyl-coenzyme M reduction, which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes methane from methyl-coenzyme M, the pathway methyl-coenzyme M reduction and in One-carbon metabolism.

Sites

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

GO - Molecular functioni

GO - Biological processi

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 Componenti: 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-methylhistidineBy similarity
Modified residuei274 – 27415-methylarginineBy 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

STRINGi79929.MTBMA_c15120.

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

        10         20         30         40         50
MDEKKLFLKA LKKKFEGEDP DEKYTNFYCF GGWEQSARKK EFTEYAKKAA
60 70 80 90 100
EKRGGIPFYN PDIGVPLGQR KLMAYRVSGT DAYVEGDDLH FVNNAAIQQM
110 120 130 140 150
VDDIKRTVIV GMDTAHAVLE KRLGVEVTPE TINEYMEAIN HALPGGAVVQ
160 170 180 190 200
EHMVEVHPGL VEDCYAKIFT GDDNLADELD KRILIDINKE FPEEQAEQLK
210 220 230 240 250
SYIGNRTYQV NRVPTIVVRT CDGGTVSRWS AMQIGMSFIS AYKLCAGEAA
260 270 280 290 300
IADFSYAAKH ADVIEMGTIM PARRARGPNE PGGVAFGTFA DIVQTSRVSD
310 320 330 340 350
DPANVSLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY
360 370 380 390 400
YGMEYVDDKY GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG
410 420 430 440 450
SQRAAVAAAA AGCSTAFATG NSNAGINGWY LSQILHKEAH SRLGFYGYDL
460 470 480 490 500
QDQCGASNSL SIRSDEGLIH ELRGPNYPNY AMNVGHQPEY AGIAQAPHAA
510 520 530 540 550
RGDAFCTNPL IKVAFADKDL AFDFTSPRKS IAAGALREFM PEGERDLIIP

AGK
Length:553
Mass (Da):60,678
Last modified:November 30, 2010 - v2
Checksum:i94CC0D641E7C8271
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21D → L AA sequence (PubMed:2269306).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL59091.1.
RefSeqiWP_013296302.1. NC_014408.1.
YP_003850404.1. NC_014408.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL59091.1.
RefSeqiWP_013296302.1. NC_014408.1.
YP_003850404.1. NC_014408.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi79929.MTBMA_c15120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000225809.
KOiK00399.
OMAiGHQPEYA.

Enzyme and pathway databases

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

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.
ProtoNetiSearch...

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: June 24, 2015
This is version 54 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.