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P07962

- MCRA_METBF

UniProt

P07962 - MCRA_METBF

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Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

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

coenzyme F4301 PublicationNote: Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme F430 is a yellow nickel porphinoid.1 Publication

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-methylhistidine1 Publication
Modified residuei285 – 28515-methylarginine1 Publication
Modified residuei465 – 46511-thioglycine1 Publication
Modified residuei472 – 4721S-methylcysteine1 Publication

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

Hexamer of two alpha, two beta, and two gamma chains.1 Publication

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6YX-ray1.60A/D2-570[»]
ProteinModelPortaliP07962.
SMRiP07962. Positions 2-569.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MAADIFSKFK KDMEVKFAQE FGSNKQTGGD ITDKTAKFLR LGPEQDPRKV
60 70 80 90 100
EMIKAGKEIA EKRGIAFYNP MMHSGAPLGQ RAITPYTISG TDIVCEPDDL
110 120 130 140 150
HYVNNAAMQQ MWDDIRRTCI VGLDMAHETL EKRLGKEVTP ETINHYLEVL
160 170 180 190 200
NHAMPGAAVV QEMMVETHPA LVDDCYVKVF TGDDALADEI DKQFLIDINK
210 220 230 240 250
EFSEEQAAQI KASIGKTSWQ AIHIPTIVSR TTDGAQTSRW AAMQIGMSFI
260 270 280 290 300
SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL
310 320 330 340 350
SDIVQTSRVS EDPAKIALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA
360 370 380 390 400
YTDDILDNNT YYDVDYINDK YNGAATVGKD NKVKASLEVV KDIATESTLY
410 420 430 440 450
GIETYEKFPT ALEDHFGGSQ RATVLAAAAG VACSLATGNA NAGLSGWYLS
460 470 480 490 500
MYLHKEAWGR LGFFGFDLQD QCGATNVLSY QGDEGLPDEL RGPNYPNYAM
510 520 530 540 550
NVGHQGGYAG IAQAAHSGRG DAFTVNPLLK VCFADDLLPF NFAEPRREFG
560 570
RGAIREFVPA GERSLVIPAK
Length:570
Mass (Da):61,962
Last modified:January 23, 2007 - v3
Checksum:i301E10CE7D449C76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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; ARG-285 AND CYS-472, THIOCARBOXYLATION 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: November 26, 2014
This is version 115 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, Reference 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