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P11558

- MCRA_METTM

UniProt

P11558 - MCRA_METTM

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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: 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

Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme F430 is a yellow nickel porphinoid.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi147 – 1471Nickel

GO - Molecular functioni

  1. coenzyme-B sulfoethylthiotransferase activity Source: MENGO
  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

BioCyciMMAR79929:GH5J-1552-MONOMER.
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: 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.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
Links Updated
X07794 Genomic DNA. Translation: CAA30639.1.
CP001710 Genomic DNA. Translation: ADL59127.1.
RefSeqiYP_003850440.1. NC_014408.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07794 Genomic DNA. Translation: CAA30639.1 .
CP001710 Genomic DNA. Translation: ADL59127.1 .
RefSeqi YP_003850440.1. NC_014408.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HBM X-ray 1.80 A/D 2-550 [» ]
1HBN X-ray 1.16 A/D 2-550 [» ]
1HBO X-ray 1.78 A/D 2-550 [» ]
1HBU X-ray 1.90 A/D 2-550 [» ]
1MRO X-ray 1.16 A/D 2-549 [» ]
3M1V X-ray 1.45 A/D 2-550 [» ]
3M2R X-ray 1.30 A/D 2-550 [» ]
3M2U X-ray 1.40 A/D 2-550 [» ]
3M2V X-ray 1.80 A/D 2-550 [» ]
3M30 X-ray 1.45 A/D 2-550 [» ]
3M32 X-ray 1.35 A/D 2-550 [» ]
3POT X-ray 1.20 A/D 1-550 [» ]
ProteinModelPortali P11558.
SMRi P11558. Positions 2-549.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADL59127 ; ADL59127 ; MTBMA_c15480 .
GeneIDi 9705257.
KEGGi mmg:MTBMA_c15480.

Phylogenomic databases

HOGENOMi HOG000225809.
KOi K00399.
OMAi MSMISAY.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .
BioCyci MMAR79929:GH5J-1552-MONOMER.

Miscellaneous databases

EvolutionaryTracei P11558.

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. "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: October 29, 2014
This is version 107 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