Skip Header

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

Methyl-coenzyme M reductase I subunit alpha

Gene

mcrA

Organism
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 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.

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 II subunit alpha (mrtA), Methyl-coenzyme M reductase II subunit gamma (mrtG), Methyl-coenzyme M reductase I subunit beta (mcrB), 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)DescriptionActionsGraphical viewLength
Metal bindingi147Nickel1

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

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 ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000000345 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001474562 – 550Methyl-coenzyme M reductase I subunit alphaAdd BLAST549

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei257Pros-methylhistidine1 Publication1
Modified residuei2715-methylarginine1 Publication1
Modified residuei4002-methylglutamine1 Publication1
Modified residuei4451-thioglycine1 Publication1
Modified residuei452S-methylcysteine1 Publication1

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

1550
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 13Combined sources7
Helixi30 – 33Combined sources4
Helixi35 – 51Combined sources17
Beta strandi60 – 62Combined sources3
Beta strandi71 – 74Combined sources4
Beta strandi80 – 82Combined sources3
Helixi83 – 86Combined sources4
Helixi88 – 90Combined sources3
Helixi92 – 102Combined sources11
Beta strandi104 – 109Combined sources6
Helixi110 – 118Combined sources9
Helixi126 – 139Combined sources14
Turni140 – 142Combined sources3
Helixi155 – 158Combined sources4
Beta strandi162 – 168Combined sources7
Helixi170 – 175Combined sources6
Helixi178 – 180Combined sources3
Helixi184 – 187Combined sources4
Helixi190 – 200Combined sources11
Beta strandi204 – 209Combined sources6
Helixi212 – 217Combined sources6
Helixi222 – 238Combined sources17
Helixi246 – 256Combined sources11
Turni257 – 259Combined sources3
Helixi269 – 271Combined sources3
Beta strandi275 – 277Combined sources3
Helixi278 – 280Combined sources3
Helixi283 – 289Combined sources7
Helixi292 – 294Combined sources3
Helixi300 – 316Combined sources17
Helixi317 – 323Combined sources7
Helixi331 – 335Combined sources5
Turni336 – 338Combined sources3
Helixi342 – 357Combined sources16
Helixi367 – 387Combined sources21
Helixi389 – 394Combined sources6
Helixi398 – 417Combined sources20
Helixi420 – 438Combined sources19
Helixi453 – 457Combined sources5
Turni462 – 464Combined sources3
Helixi468 – 470Combined sources3
Helixi476 – 478Combined sources3
Beta strandi482 – 484Combined sources3
Helixi485 – 499Combined sources15
Helixi507 – 512Combined sources6
Beta strandi518 – 520Combined sources3
Helixi525 – 533Combined sources9
Helixi544 – 546Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5A0YX-ray1.10A/D1-550[»]
5G0RX-ray1.25A/D1-550[»]
ProteinModelPortaliP11558.
SMRiP11558.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11558.

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.

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.

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5A0YX-ray1.10A/D1-550[»]
5G0RX-ray1.25A/D1-550[»]
ProteinModelPortaliP11558.
SMRiP11558.
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

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

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.
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...

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: November 2, 2016
This is version 122 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

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.