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Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

Organism
Methanothermus fervidus
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 bindingi150 – 1501NickelBy 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
OrganismiMethanothermus fervidus
Taxonomic identifieri2180 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Methyl-coenzyme M reductase subunit alphaPRO_0000147450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601Pros-methylhistidineBy similarity
Modified residuei274 – 27415-methylarginineBy similarity

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP12971.
SMRiP12971. 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.

P12971-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEERKKLFV DALRKKFKEE PKERKTTFYT LGGWKQSERK KEFVEYGKKV
60 70 80 90 100
AKERGIPAYN PDIGTPLGQR VLMPYQVSTT DTFVEGDDLH FVNNLAMQQF
110 120 130 140 150
WDDIRRTVIV GLNHAHRILE RSLGKEVTPE TINHYLETVN HAMPGAAVVQ
160 170 180 190 200
EHMVETHPGL TADSYVKVFT GNDELADEIE SCYLIDINKQ FPEHQAEQLK
210 220 230 240 250
KAIGHTIWQA VRIPTIVSRT CDGATTSRWS AMQIGMSMIS AYKQAAGEAA
260 270 280 290 300
TADFAYAAKH AEVIHLGTFL PVRRARGENE LGGVPFGFLA DIVQSSRVHY
310 320 330 340 350
EDPVRVALDV VASGAMLYDQ IWLGSYMSGG VGFTQYATAS YTDNILDDFT
360 370 380 390 400
YYGKEYVEDK YGGLAEAPHD FDTILDVATE VTLYSLDQYE EYPTLMEDHF
410 420 430 440 450
GGSQRAAIAA AASGCSTAFA AGNAQAGLSG WYLSQILHKE CHARLGFYGY
460 470 480 490 500
DLQDQCGAAN TYSIRSDEGL PAELRGPNYP NYAMNVGHLG EYAGIVQAAH
510 520 530 540 550
IARGDADSLN PLVKVAFADD NLPFDWTNPR GEFAKGALRE FEPEGERDLI

RPAGK
Length:555
Mass (Da):61,550
Last modified:October 1, 1989 - v1
Checksum:iC2517AB56DA53D72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03375 Genomic DNA. Translation: AAA72197.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03375 Genomic DNA. Translation: AAA72197.1.

3D structure databases

ProteinModelPortaliP12971.
SMRiP12971. 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. "Structure and comparative analysis of the genes encoding component C of methyl coenzyme M reductase in the extremely thermophilic archaebacterium Methanothermus fervidus."
    Weil C.F., Cram D.S., Sherf B.A., Reeve J.N.
    J. Bacteriol. 170:4718-4726(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiMCRA_METFE
AccessioniPrimary (citable) accession number: P12971
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 26, 2014
This is version 79 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.