SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07962

- MCRA_METBF

UniProt

P07962 - MCRA_METBF

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methyl-coenzyme M reductase subunit alpha

Gene
mcrA, Mbar_A0893
Organism
Methanosarcina barkeri (strain Fusaro / DSM 804)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611Nickel

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

BioCyciMBAR269797:GHUW-907-MONOMER.
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
Ordered Locus Names:Mbar_A0893
OrganismiMethanosarcina barkeri (strain Fusaro / DSM 804)
Taxonomic identifieri269797 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000008156: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 570569Methyl-coenzyme M reductase subunit alphaPRO_0000147449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei271 – 2711Pros-methylhistidine
Modified residuei285 – 28515-methylarginine
Modified residuei465 – 46511-thioglycine
Modified residuei472 – 4721S-methylcysteine

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi269797.Mbar_A0893.

Structurei

Secondary structure

1
570
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1715
Helixi43 – 453
Helixi47 – 6317
Helixi70 – 723
Beta strandi73 – 764
Beta strandi86 – 883
Helixi97 – 1004
Helixi102 – 1043
Helixi106 – 11611
Beta strandi118 – 1236
Helixi124 – 13411
Helixi140 – 15314
Turni154 – 1563
Helixi169 – 1713
Beta strandi176 – 1827
Helixi184 – 1874
Helixi192 – 1943
Helixi198 – 2014
Helixi204 – 21411
Beta strandi218 – 2236
Helixi226 – 2316
Helixi236 – 25217
Helixi260 – 27011
Turni271 – 2733
Helixi283 – 2853
Beta strandi289 – 2913
Helixi292 – 2943
Helixi297 – 3037
Helixi306 – 3094
Helixi313 – 33018
Helixi331 – 3366
Helixi344 – 3485
Turni349 – 3513
Helixi355 – 37016
Beta strandi379 – 3813
Helixi387 – 40721
Helixi409 – 4146
Helixi418 – 43720
Helixi440 – 45819
Helixi468 – 4714
Helixi473 – 4775
Turni482 – 4843
Turni488 – 4903
Helixi496 – 4983
Beta strandi502 – 5043
Helixi505 – 51713
Turni518 – 5203
Helixi527 – 5326
Beta strandi538 – 5403
Helixi545 – 5539
Helixi564 – 5663

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6YX-ray1.60A/D2-570[»]
ProteinModelPortaliP07962.
SMRiP07962. Positions 2-569.

Miscellaneous databases

EvolutionaryTraceiP07962.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG4058.
HOGENOMiHOG000225809.
KOiK00399.
OMAiAHSARGD.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07962-1 [UniParc]FASTAAdd to Basket

« Hide

MAADIFSKFK KDMEVKFAQE FGSNKQTGGD ITDKTAKFLR LGPEQDPRKV    50
EMIKAGKEIA EKRGIAFYNP MMHSGAPLGQ RAITPYTISG TDIVCEPDDL 100
HYVNNAAMQQ MWDDIRRTCI VGLDMAHETL EKRLGKEVTP ETINHYLEVL 150
NHAMPGAAVV QEMMVETHPA LVDDCYVKVF TGDDALADEI DKQFLIDINK 200
EFSEEQAAQI KASIGKTSWQ AIHIPTIVSR TTDGAQTSRW AAMQIGMSFI 250
SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL 300
SDIVQTSRVS EDPAKIALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA 350
YTDDILDNNT YYDVDYINDK YNGAATVGKD NKVKASLEVV KDIATESTLY 400
GIETYEKFPT ALEDHFGGSQ RATVLAAAAG VACSLATGNA NAGLSGWYLS 450
MYLHKEAWGR LGFFGFDLQD QCGATNVLSY QGDEGLPDEL RGPNYPNYAM 500
NVGHQGGYAG IAQAAHSGRG DAFTVNPLLK VCFADDLLPF NFAEPRREFG 550
RGAIREFVPA GERSLVIPAK 570
Length:570
Mass (Da):61,962
Last modified:January 23, 2007 - v3
Checksum:i301E10CE7D449C76
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00158 Genomic DNA. Translation: CAA68357.1.
CP000099 Genomic DNA. Translation: AAZ69867.1.
PIRiE29525.
RefSeqiWP_011305916.1. NC_007355.1.
YP_304447.1. NC_007355.1.

Genome annotation databases

EnsemblBacteriaiAAZ69867; AAZ69867; Mbar_A0893.
GeneIDi3625938.
KEGGimba:Mbar_A0893.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00158 Genomic DNA. Translation: CAA68357.1 .
CP000099 Genomic DNA. Translation: AAZ69867.1 .
PIRi E29525.
RefSeqi WP_011305916.1. NC_007355.1.
YP_304447.1. NC_007355.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E6Y X-ray 1.60 A/D 2-570 [» ]
ProteinModelPortali P07962.
SMRi P07962. Positions 2-569.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 269797.Mbar_A0893.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ69867 ; AAZ69867 ; Mbar_A0893 .
GeneIDi 3625938.
KEGGi mba:Mbar_A0893.

Phylogenomic databases

eggNOGi COG4058.
HOGENOMi HOG000225809.
KOi K00399.
OMAi AHSARGD.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .
BioCyci MBAR269797:GHUW-907-MONOMER.

Miscellaneous databases

EvolutionaryTracei P07962.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of the methyl coenzyme M reductase gene cluster from Methanosarcina barkeri."
    Bokranz M., Klein A.
    Nucleic Acids Res. 15:4350-4351(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
    Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
    J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Fusaro / DSM 804.
  3. "Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation."
    Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.
    J. Mol. Biol. 303:329-344(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH COENZYME F430, COFACTOR, METHYLATION AT HIS-271, METHYLATION AT ARG-285, METHYLATION AT CYS-472, THIOLATION AT GLY-465, SUBUNIT.

Entry informationi

Entry nameiMCRA_METBF
AccessioniPrimary (citable) accession number: P07962
Secondary accession number(s): Q46E25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi