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Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

Organism
Methanococcus vannielii
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

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 subunit beta (mcrB), Methyl-coenzyme M reductase subunit alpha (mcrA), Methyl-coenzyme M reductase 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 bindingi151 – 1511NickelBy 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

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 vannielii
Taxonomic identifieri2187 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Methyl-coenzyme M reductase subunit alphaPRO_0000147460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei261 – 2611Pros-methylhistidineBy similarity
Modified residuei275 – 27515-methylarginineBy similarity

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi406327.Mevan_0872.

Structurei

3D structure databases

ProteinModelPortaliP07961.
SMRiP07961. Positions 7-552.
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.

P07961-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAEKRLFLK ALKEKFEEDP KEKYTKFYTY GGWEQSVRKR EFVAANEKVL
60 70 80 90 100
AEKRQGVPLY NPDIGVPLGQ RKLMPYKLSG TDSYCEGDDL HFMNNAAIQQ
110 120 130 140 150
LWDDIRRTVV VGMDTAHSVL EKRLGVEVTP ETINEYMHTI NHALSGGAVV
160 170 180 190 200
QEHMVEVHPS LAWDSYARIF TGDDELAAEL DSRFLIDINK LFPAEQAEAL
210 220 230 240 250
KKAIGKKTYQ VSRVPSLVGR VCDGGTISRW SAMQIGMSFI TAYKLCAGEA
260 270 280 290 300
ATADFSYASK HADVIQMGNA LPGRRARGPN EPGGIQFGIL SDVVQTTRVS
310 320 330 340 350
DDPVEQSLEV VAAGAALYDQ IWLGAYMSGG VGFTQYATAA YTDDILDDFS
360 370 380 390 400
YYALDYVEKK YGRMGTKATM DVVEDIASEV TLYSLEQYDE YPALLEDHFG
410 420 430 440 450
GSQRAAVAAA ASGIGVCMAT GNSNAGVNGW YLSQILHKEY HSRLGFYGYD
460 470 480 490 500
LQDQCGASNS LAIRNDESAP LELRGPNYPN YAMNVGHQGE YAGIAQAAHS
510 520 530 540 550
ARGDAFAMSA LIKVAFADPM LVFDFSKPRK EFARGALREF DAAGERDVIL

PAK
Length:553
Mass (Da):60,838
Last modified:August 1, 1988 - v1
Checksum:i7B91F2DDA4B98489
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16893 Genomic DNA. Translation: AAA72598.1.
PIRiE27793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16893 Genomic DNA. Translation: AAA72598.1.
PIRiE27793.

3D structure databases

ProteinModelPortaliP07961.
SMRiP07961. Positions 7-552.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi406327.Mevan_0872.

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 expression of the genes, mcrBDCGA, which encode the subunits of component C of methyl coenzyme M reductase in Methanococcus vannielii."
    Cram D.S., Sherf B.A., Libby R.T., Mattaliano R.J., Ramachandran K.L., Reeve J.N.
    Proc. Natl. Acad. Sci. U.S.A. 84:3992-3996(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiMCRA_METVA
AccessioniPrimary (citable) accession number: P07961
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 24, 2015
This is version 81 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.