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Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

Organism
Methanococcus voltae
Status
Reviewed-Annotation score: 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

coenzyme F430By similarityNote: 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 – 1521NickelBy 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

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 alphaPRO_0000147461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 2621Pros-methylhistidineBy similarity
Modified residuei276 – 27615-methylarginineBy 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.
ModBaseiSearch...
MobiDBiSearch...

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

« Hide

        10         20         30         40         50
MEAEKRLFLK ALKEKFEEDP KEKFTKFYTY GGWQQSARKQ EFVSENEKIV
60 70 80 90 100
AEKRGGIPMY NPDIGVPLGQ RKLMPYKISN TDTYVEGDDL HFMNNAAIQQ
110 120 130 140 150
LWDDIRRTVI VGMDTAHMVL EKRLGVEVTP ETINEYMHTI NHSLPGGAAV
160 170 180 190 200
VQEHMVEVHP SLAWDCYAKI FTGDDELADE LDDRFVIDIN KLFPEEQAEA
210 220 230 240 250
SKAAIGKKTY QVSRVPSLVG RVCDGGTISR WSAMQIGMSF ITAYKLCAGE
260 270 280 290 300
AAIADFSYAA KHADVIQMGN ALLGRRARGP NELGGVRFGI LSDVVQTTRV
310 320 330 340 350
SDDPVEQSLE VVATGAALYD QIWLGSYMSG GVGFTQYATA SYTDDILDDF
360 370 380 390 400
SYYGYEYVEK KYGRCGTKAT MDVVEDIASE VTLYALEQYD EYPALLEDHF
410 420 430 440 450
GGSQRAAVAA AAAGISVCMA TGNSNAGVNG WYLSQILHKE YHSRLGFYGY
460 470 480 490 500
DLQDQCGASN SLAIRNDEAS PLELRGPNYP NYAMNVGHQG EYAGIAQSAH
510 520 530 540 550
SARGDAFATN ALIKVAFADP SLVFDFSKPR KEIARGALRE FEAAGERDPI

LPAKI
Length:555
Mass (Da):61,227
Last modified:October 1, 1989 - v1
Checksum:iDCBCE5DC91EA69D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07793 Genomic DNA. Translation: CAA30633.1.
PIRiS03261.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07793 Genomic DNA. Translation: CAA30633.1.
PIRiS03261.

3D structure databases

ProteinModelPortaliP11559.
SMRiP11559. Positions 7-553.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

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

  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: November 26, 2014
This is version 80 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

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.