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Protein

Methyl-coenzyme M reductase subunit alpha

Gene

mcrA

Organism
Methanosarcina barkeri (strain Fusaro / DSM 804)
Status
Reviewed-Annotation score: 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: 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 gamma (mcrG), Methyl-coenzyme M reductase subunit beta (mcrB), Methyl-coenzyme M reductase subunit alpha (mcrA)
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)DescriptionActionsGraphical viewLength
Metal bindingi161Nickel1

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

BRENDAi2.8.4.1. 3250.
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
Proteomesi
  • UP000008156 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001474492 – 570Methyl-coenzyme M reductase subunit alphaAdd BLAST569

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei271Pros-methylhistidine1 Publication1
Modified residuei2855-methylarginine1 Publication1
Modified residuei4651-thioglycine1 Publication1
Modified residuei472S-methylcysteine1 Publication1

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

1570
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 17Combined sources15
Helixi43 – 45Combined sources3
Helixi47 – 63Combined sources17
Helixi70 – 72Combined sources3
Beta strandi73 – 76Combined sources4
Beta strandi86 – 88Combined sources3
Helixi97 – 100Combined sources4
Helixi102 – 104Combined sources3
Helixi106 – 116Combined sources11
Beta strandi118 – 123Combined sources6
Helixi124 – 134Combined sources11
Helixi140 – 153Combined sources14
Turni154 – 156Combined sources3
Helixi169 – 171Combined sources3
Beta strandi176 – 182Combined sources7
Helixi184 – 187Combined sources4
Helixi192 – 194Combined sources3
Helixi198 – 201Combined sources4
Helixi204 – 214Combined sources11
Beta strandi218 – 223Combined sources6
Helixi226 – 231Combined sources6
Helixi236 – 252Combined sources17
Helixi260 – 270Combined sources11
Turni271 – 273Combined sources3
Helixi283 – 285Combined sources3
Beta strandi289 – 291Combined sources3
Helixi292 – 294Combined sources3
Helixi297 – 303Combined sources7
Helixi306 – 309Combined sources4
Helixi313 – 330Combined sources18
Helixi331 – 336Combined sources6
Helixi344 – 348Combined sources5
Turni349 – 351Combined sources3
Helixi355 – 370Combined sources16
Beta strandi379 – 381Combined sources3
Helixi387 – 407Combined sources21
Helixi409 – 414Combined sources6
Helixi418 – 437Combined sources20
Helixi440 – 458Combined sources19
Helixi468 – 471Combined sources4
Helixi473 – 477Combined sources5
Turni482 – 484Combined sources3
Turni488 – 490Combined sources3
Helixi496 – 498Combined sources3
Beta strandi502 – 504Combined sources3
Helixi505 – 517Combined sources13
Turni518 – 520Combined sources3
Helixi527 – 532Combined sources6
Beta strandi538 – 540Combined sources3
Helixi545 – 553Combined sources9
Helixi564 – 566Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP07962.

Family & Domainsi

Phylogenomic databases

eggNOGiarCOG04857. Archaea.
COG4058. LUCA.
HOGENOMiHOG000225809.
KOiK00399.
OMAiGLDMAHE.

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.

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.
PIRiE29525.
RefSeqiWP_011305916.1. NC_007355.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi269797.Mbar_A0893.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiarCOG04857. Archaea.
COG4058. LUCA.
HOGENOMiHOG000225809.
KOiK00399.
OMAiGLDMAHE.

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.
BRENDAi2.8.4.1. 3250.

Miscellaneous databases

EvolutionaryTraceiP07962.

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...

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 2, 2016
This is version 124 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

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 one 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.