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P11559

- MCRA_METVO

UniProt

P11559 - MCRA_METVO

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Protein
Methyl-coenzyme M reductase subunit alpha
Gene
mcrA
Organism
Methanococcus voltae
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 bindingi152 – 1521Nickel By similarity

GO - Molecular functioni

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

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

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
OrganismiMethanococcus voltae
Taxonomic identifieri2188 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Methyl-coenzyme M reductase subunit alpha
PRO_0000147461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 2621Pros-methylhistidine By similarity
Modified residuei276 – 27615-methylarginine By similarity

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP11559.
SMRiP11559. Positions 7-553.

Family & Domainsi

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.

P11559-1 [UniParc]FASTAAdd to Basket

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MEAEKRLFLK ALKEKFEEDP KEKFTKFYTY GGWQQSARKQ EFVSENEKIV    50
AEKRGGIPMY NPDIGVPLGQ RKLMPYKISN TDTYVEGDDL HFMNNAAIQQ 100
LWDDIRRTVI VGMDTAHMVL EKRLGVEVTP ETINEYMHTI NHSLPGGAAV 150
VQEHMVEVHP SLAWDCYAKI FTGDDELADE LDDRFVIDIN KLFPEEQAEA 200
SKAAIGKKTY QVSRVPSLVG RVCDGGTISR WSAMQIGMSF ITAYKLCAGE 250
AAIADFSYAA KHADVIQMGN ALLGRRARGP NELGGVRFGI LSDVVQTTRV 300
SDDPVEQSLE VVATGAALYD QIWLGSYMSG GVGFTQYATA SYTDDILDDF 350
SYYGYEYVEK KYGRCGTKAT MDVVEDIASE VTLYALEQYD EYPALLEDHF 400
GGSQRAAVAA AAAGISVCMA TGNSNAGVNG WYLSQILHKE YHSRLGFYGY 450
DLQDQCGASN SLAIRNDEAS PLELRGPNYP NYAMNVGHQG EYAGIAQSAH 500
SARGDAFATN ALIKVAFADP SLVFDFSKPR KEIARGALRE FEAAGERDPI 550
LPAKI 555
Length:555
Mass (Da):61,227
Last modified:October 1, 1989 - v1
Checksum:iDCBCE5DC91EA69D5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07793 Genomic DNA. Translation: CAA30633.1.
PIRiS03261.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07793 Genomic DNA. Translation: CAA30633.1 .
PIRi S03261.

3D structure databases

ProteinModelPortali P11559.
SMRi P11559. Positions 7-553.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .

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

  1. "Comparative analysis of genes encoding methyl coenzyme M reductase in methanogenic bacteria."
    Klein A., Allmansberger R., Bokranz M., Knaub S., Mueller B., Muth E.
    Mol. Gen. Genet. 213:409-420(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS.

Entry informationi

Entry nameiMCRA_METVO
AccessioniPrimary (citable) accession number: P11559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

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