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Protein

Methyl-coenzyme M reductase II subunit alpha

Gene

mrtA

Organism
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 3 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 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)DescriptionActionsGraphical viewLength
Metal bindingi150NickelBy similarity1

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

UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase II subunit alpha (EC:2.8.4.1)
Short name:
MCR II alpha
Gene namesi
Name:mrtA
Ordered Locus Names:MTBMA_c15120
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
ChainiPRO_00001474581 – 553Methyl-coenzyme M reductase II subunit alphaAdd BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei260Pros-methylhistidineBy similarity1
Modified residuei2745-methylarginineBy similarity1

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_c15120.

Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 14Combined sources7
Turni15 – 17Combined sources3
Helixi32 – 35Combined sources4
Helixi37 – 48Combined sources12
Turni49 – 55Combined sources7
Beta strandi63 – 65Combined sources3
Beta strandi74 – 77Combined sources4
Beta strandi83 – 85Combined sources3
Helixi86 – 89Combined sources4
Turni91 – 93Combined sources3
Helixi95 – 105Combined sources11
Beta strandi107 – 112Combined sources6
Helixi113 – 121Combined sources9
Helixi129 – 142Combined sources14
Turni143 – 145Combined sources3
Helixi158 – 160Combined sources3
Beta strandi165 – 171Combined sources7
Helixi173 – 178Combined sources6
Helixi181 – 183Combined sources3
Helixi187 – 190Combined sources4
Helixi193 – 203Combined sources11
Beta strandi207 – 212Combined sources6
Helixi215 – 220Combined sources6
Helixi225 – 241Combined sources17
Helixi251 – 259Combined sources9
Turni260 – 262Combined sources3
Helixi272 – 274Combined sources3
Beta strandi278 – 280Combined sources3
Helixi281 – 283Combined sources3
Helixi286 – 292Combined sources7
Helixi295 – 297Combined sources3
Helixi302 – 317Combined sources16
Helixi318 – 325Combined sources8
Helixi333 – 337Combined sources5
Turni338 – 340Combined sources3
Helixi344 – 359Combined sources16
Helixi369 – 389Combined sources21
Helixi391 – 396Combined sources6
Helixi400 – 419Combined sources20
Helixi422 – 440Combined sources19
Helixi455 – 459Combined sources5
Turni464 – 466Combined sources3
Helixi470 – 472Combined sources3
Helixi478 – 480Combined sources3
Beta strandi484 – 486Combined sources3
Helixi487 – 501Combined sources15
Helixi509 – 514Combined sources6
Beta strandi520 – 522Combined sources3
Helixi527 – 535Combined sources9
Helixi546 – 548Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A8RX-ray2.15A/D/G/J1-553[»]
SMRiP58815.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiarCOG04857. Archaea.
COG4058. LUCA.
HOGENOMiHOG000225809.
KOiK00399.
OMAiQRKLMAY.

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.

P58815-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEKKLFLKA LKKKFEGEDP DEKYTNFYCF GGWEQSARKK EFTEYAKKAA
60 70 80 90 100
EKRGGIPFYN PDIGVPLGQR KLMAYRVSGT DAYVEGDDLH FVNNAAIQQM
110 120 130 140 150
VDDIKRTVIV GMDTAHAVLE KRLGVEVTPE TINEYMEAIN HALPGGAVVQ
160 170 180 190 200
EHMVEVHPGL VEDCYAKIFT GDDNLADELD KRILIDINKE FPEEQAEQLK
210 220 230 240 250
SYIGNRTYQV NRVPTIVVRT CDGGTVSRWS AMQIGMSFIS AYKLCAGEAA
260 270 280 290 300
IADFSYAAKH ADVIEMGTIM PARRARGPNE PGGVAFGTFA DIVQTSRVSD
310 320 330 340 350
DPANVSLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY
360 370 380 390 400
YGMEYVDDKY GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG
410 420 430 440 450
SQRAAVAAAA AGCSTAFATG NSNAGINGWY LSQILHKEAH SRLGFYGYDL
460 470 480 490 500
QDQCGASNSL SIRSDEGLIH ELRGPNYPNY AMNVGHQPEY AGIAQAPHAA
510 520 530 540 550
RGDAFCTNPL IKVAFADKDL AFDFTSPRKS IAAGALREFM PEGERDLIIP

AGK
Length:553
Mass (Da):60,678
Last modified:November 30, 2010 - v2
Checksum:i94CC0D641E7C8271
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2D → L AA sequence (PubMed:2269306).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL59091.1.
RefSeqiWP_013296302.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL59091; ADL59091; MTBMA_c15120.
GeneIDi9705221.
KEGGimmg:MTBMA_c15120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL59091.1.
RefSeqiWP_013296302.1. NC_014408.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A8RX-ray2.15A/D/G/J1-553[»]
SMRiP58815.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi79929.MTBMA_c15120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADL59091; ADL59091; MTBMA_c15120.
GeneIDi9705221.
KEGGimmg:MTBMA_c15120.

Phylogenomic databases

eggNOGiarCOG04857. Archaea.
COG4058. LUCA.
HOGENOMiHOG000225809.
KOiK00399.
OMAiQRKLMAY.

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

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 nameiMCRX_METTM
AccessioniPrimary (citable) accession number: P58815
Secondary accession number(s): D9PXZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: November 30, 2010
Last modified: November 30, 2016
This is version 59 of the entry and version 2 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.