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Protein

Methyl-coenzyme M reductase I subunit alpha

Gene

mcrA

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 5 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 F430Note: Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme F430 is a yellow nickel porphinoid.

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 II subunit alpha (mrtA), Methyl-coenzyme M reductase I subunit beta (mcrB), Methyl-coenzyme M reductase II subunit gamma (mrtG), Methyl-coenzyme M reductase I subunit alpha (mcrA), Methyl-coenzyme M reductase I 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 bindingi147 – 1471Nickel

GO - Molecular functioni

  • coenzyme-B sulfoethylthiotransferase activity Source: MENGO
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

BioCyciMMAR79929:GH5J-1552-MONOMER.
BRENDAi2.8.4.1. 7427.
UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase I subunit alpha (EC:2.8.4.1)
Short name:
MCR I alpha
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase alpha
Gene namesi
Name:mcrA
Ordered Locus Names:MTBMA_c15480
OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000000345 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 550549Methyl-coenzyme M reductase I subunit alphaPRO_0000147456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571Pros-methylhistidine1 Publication
Modified residuei271 – 27115-methylarginine1 Publication
Modified residuei400 – 40012-methylglutamine1 Publication
Modified residuei445 – 44511-thioglycine1 Publication
Modified residuei452 – 4521S-methylcysteine1 Publication

Keywords - PTMi

Methylation

Expressioni

Developmental stagei

There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi79929.MTBMA_c15480.

Structurei

Secondary structure

1
550
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 137Combined sources
Helixi30 – 334Combined sources
Helixi35 – 5117Combined sources
Beta strandi60 – 623Combined sources
Beta strandi71 – 744Combined sources
Beta strandi80 – 823Combined sources
Helixi83 – 864Combined sources
Helixi88 – 903Combined sources
Helixi92 – 10211Combined sources
Beta strandi104 – 1096Combined sources
Helixi110 – 1189Combined sources
Helixi126 – 13914Combined sources
Turni140 – 1423Combined sources
Helixi155 – 1584Combined sources
Beta strandi162 – 1687Combined sources
Helixi170 – 1756Combined sources
Helixi178 – 1803Combined sources
Helixi184 – 1874Combined sources
Helixi190 – 20011Combined sources
Beta strandi204 – 2096Combined sources
Helixi212 – 2176Combined sources
Helixi222 – 23918Combined sources
Helixi246 – 25611Combined sources
Turni257 – 2593Combined sources
Helixi269 – 2713Combined sources
Beta strandi275 – 2773Combined sources
Helixi278 – 2803Combined sources
Helixi283 – 2897Combined sources
Helixi292 – 2954Combined sources
Helixi300 – 31617Combined sources
Helixi317 – 3237Combined sources
Helixi331 – 3355Combined sources
Turni336 – 3383Combined sources
Helixi342 – 35716Combined sources
Helixi367 – 38721Combined sources
Helixi389 – 3946Combined sources
Helixi398 – 41720Combined sources
Helixi420 – 43819Combined sources
Helixi448 – 45710Combined sources
Turni462 – 4643Combined sources
Helixi468 – 4703Combined sources
Helixi476 – 4783Combined sources
Beta strandi482 – 4843Combined sources
Helixi485 – 49915Combined sources
Helixi507 – 5126Combined sources
Beta strandi518 – 5203Combined sources
Helixi525 – 5339Combined sources
Helixi544 – 5463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBMX-ray1.80A/D2-550[»]
1HBNX-ray1.16A/D2-550[»]
1HBOX-ray1.78A/D2-550[»]
1HBUX-ray1.90A/D2-550[»]
1MROX-ray1.16A/D2-549[»]
3M1VX-ray1.45A/D2-550[»]
3M2RX-ray1.30A/D2-550[»]
3M2UX-ray1.40A/D2-550[»]
3M2VX-ray1.80A/D2-550[»]
3M30X-ray1.45A/D2-550[»]
3M32X-ray1.35A/D2-550[»]
3POTX-ray1.20A/D1-550[»]
ProteinModelPortaliP11558.
SMRiP11558. Positions 2-549.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11558.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000225809.
KOiK00399.
OMAiMSMISAY.

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.

P11558-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK
60 70 80 90 100
RGIPQYNPDI GTPLGQRVLM PYQVSTTDTY VEGDDLHFVN NAAMQQMWDD
110 120 130 140 150
IRRTVIVGLN HAHAVIEKRL GKEVTPETIT HYLETVNHAM PGAAVVQEHM
160 170 180 190 200
VETHPALVAD SYVKVFTGND EIADEIDPAF VIDINKQFPE DQAETLKAEV
210 220 230 240 250
GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK QAAGEAATGD
260 270 280 290 300
FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP
310 320 330 340 350
VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG
360 370 380 390 400
KEYVEDKYGL CEAPNNMDTV LDVATEVTFY GLEQYEEYPA LLEDQFGGSQ
410 420 430 440 450
RAAVVAAAAG CSTAFATGNA QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD
460 470 480 490 500
QCGASNVFSI RGDEGLPLEL RGPNYPNYAM NVGHQGEYAG ISQAPHAARG
510 520 530 540 550
DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA GERALITPAK
Length:550
Mass (Da):60,511
Last modified:January 23, 2007 - v3
Checksum:iD55A724B6CA9EFEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07794 Genomic DNA. Translation: CAA30639.1.
CP001710 Genomic DNA. Translation: ADL59127.1.
RefSeqiWP_013296337.1. NC_014408.1.
YP_003850440.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL59127; ADL59127; MTBMA_c15480.
GeneIDi9705257.
KEGGimmg:MTBMA_c15480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07794 Genomic DNA. Translation: CAA30639.1.
CP001710 Genomic DNA. Translation: ADL59127.1.
RefSeqiWP_013296337.1. NC_014408.1.
YP_003850440.1. NC_014408.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBMX-ray1.80A/D2-550[»]
1HBNX-ray1.16A/D2-550[»]
1HBOX-ray1.78A/D2-550[»]
1HBUX-ray1.90A/D2-550[»]
1MROX-ray1.16A/D2-549[»]
3M1VX-ray1.45A/D2-550[»]
3M2RX-ray1.30A/D2-550[»]
3M2UX-ray1.40A/D2-550[»]
3M2VX-ray1.80A/D2-550[»]
3M30X-ray1.45A/D2-550[»]
3M32X-ray1.35A/D2-550[»]
3POTX-ray1.20A/D1-550[»]
ProteinModelPortaliP11558.
SMRiP11558. Positions 2-549.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi79929.MTBMA_c15480.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADL59127; ADL59127; MTBMA_c15480.
GeneIDi9705257.
KEGGimmg:MTBMA_c15480.

Phylogenomic databases

HOGENOMiHOG000225809.
KOiK00399.
OMAiMSMISAY.

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.
BioCyciMMAR79929:GH5J-1552-MONOMER.
BRENDAi2.8.4.1. 7427.

Miscellaneous databases

EvolutionaryTraceiP11558.

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

« Hide 'large scale' publications
  1. "Cloning and characterization of the methyl coenzyme M reductase genes from Methanobacterium thermoautotrophicum."
    Bokranz M., Baeumner G., Allmansberger R., Ankel-Fuchs D., Klein A.
    J. Bacteriol. 170:568-577(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  2. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
    Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
    J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  3. "Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H."
    Rospert S., Linder D., Ellermann J., Thauer R.K.
    Eur. J. Biochem. 194:871-877(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19.
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  4. "The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase."
    Selmer T., Kahnt J., Goubeaud M., Shima S., Grabarse W., Ermler U., Thauer R.K.
    J. Biol. Chem. 275:3755-3760(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT HIS-257; ARG-271; GLN-400 AND CYS-452, THIOCARBOXYLATION AT GLY-445.
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  5. "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation."
    Ermler U., Grabarse W., Shima S., Goubeaud M., Thauer R.K.
    Science 278:1457-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
  6. "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding."
    Grabarse W., Mahlert F., Duin E.C., Goubeaud M., Shima S., Thauer R.K., Lamzin V., Ermler U.
    J. Mol. Biol. 309:315-330(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).
    Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Entry informationi

Entry nameiMCRA_METTM
AccessioniPrimary (citable) accession number: P11558
Secondary accession number(s): D9PY29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: June 24, 2015
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, Direct protein sequencing

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

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.