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P07961

- MCRA_METVA

UniProt

P07961 - MCRA_METVA

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Protein
Methyl-coenzyme M reductase subunit alpha
Gene
mcrA
Organism
Methanococcus vannielii
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 bindingi151 – 1511Nickel By 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 vannielii
Taxonomic identifieri2187 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Methyl-coenzyme M reductase subunit alpha
PRO_0000147460Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei261 – 2611Pros-methylhistidine By similarity
Modified residuei275 – 27515-methylarginine By similarity

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP07961.
SMRiP07961. Positions 7-552.

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

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MEAEKRLFLK ALKEKFEEDP KEKYTKFYTY GGWEQSVRKR EFVAANEKVL    50
AEKRQGVPLY NPDIGVPLGQ RKLMPYKLSG TDSYCEGDDL HFMNNAAIQQ 100
LWDDIRRTVV VGMDTAHSVL EKRLGVEVTP ETINEYMHTI NHALSGGAVV 150
QEHMVEVHPS LAWDSYARIF TGDDELAAEL DSRFLIDINK LFPAEQAEAL 200
KKAIGKKTYQ VSRVPSLVGR VCDGGTISRW SAMQIGMSFI TAYKLCAGEA 250
ATADFSYASK HADVIQMGNA LPGRRARGPN EPGGIQFGIL SDVVQTTRVS 300
DDPVEQSLEV VAAGAALYDQ IWLGAYMSGG VGFTQYATAA YTDDILDDFS 350
YYALDYVEKK YGRMGTKATM DVVEDIASEV TLYSLEQYDE YPALLEDHFG 400
GSQRAAVAAA ASGIGVCMAT GNSNAGVNGW YLSQILHKEY HSRLGFYGYD 450
LQDQCGASNS LAIRNDESAP LELRGPNYPN YAMNVGHQGE YAGIAQAAHS 500
ARGDAFAMSA LIKVAFADPM LVFDFSKPRK EFARGALREF DAAGERDVIL 550
PAK 553
Length:553
Mass (Da):60,838
Last modified:August 1, 1988 - v1
Checksum:i7B91F2DDA4B98489
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16893 Genomic DNA. Translation: AAA72598.1.
PIRiE27793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16893 Genomic DNA. Translation: AAA72598.1 .
PIRi E27793.

3D structure databases

ProteinModelPortali P07961.
SMRi P07961. Positions 7-552.
ModBasei Search...
MobiDBi 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. "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: 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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