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Protein

Methyl-coenzyme M reductase I subunit beta

Gene

mcrB

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.

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.

GO - Molecular functioni

  • coenzyme-B sulfoethylthiotransferase activity Source: MENGO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Enzyme and pathway databases

BRENDAi2.8.4.1. 7427.
UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase I subunit beta (EC:2.8.4.1)
Short name:
MCR I beta
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase beta
Gene namesi
Name:mcrB
Ordered Locus Names:MTBMA_c15520
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_00001474682 – 443Methyl-coenzyme M reductase I subunit betaAdd BLAST442

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_c15520.

Structurei

Secondary structure

1443
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Beta strandi17 – 23Combined sources7
Helixi24 – 27Combined sources4
Turni29 – 31Combined sources3
Helixi33 – 44Combined sources12
Beta strandi45 – 49Combined sources5
Helixi50 – 59Combined sources10
Helixi79 – 81Combined sources3
Helixi82 – 93Combined sources12
Beta strandi102 – 106Combined sources5
Helixi107 – 109Combined sources3
Beta strandi111 – 115Combined sources5
Helixi118 – 122Combined sources5
Beta strandi124 – 127Combined sources4
Helixi129 – 146Combined sources18
Turni150 – 152Combined sources3
Helixi153 – 161Combined sources9
Turni162 – 166Combined sources5
Beta strandi167 – 169Combined sources3
Beta strandi174 – 176Combined sources3
Helixi182 – 184Combined sources3
Helixi191 – 193Combined sources3
Helixi197 – 203Combined sources7
Turni204 – 206Combined sources3
Helixi208 – 225Combined sources18
Turni226 – 229Combined sources4
Helixi231 – 233Combined sources3
Helixi234 – 245Combined sources12
Helixi248 – 250Combined sources3
Helixi251 – 259Combined sources9
Turni260 – 262Combined sources3
Helixi265 – 278Combined sources14
Beta strandi283 – 288Combined sources6
Beta strandi291 – 295Combined sources5
Helixi299 – 321Combined sources23
Helixi324 – 326Combined sources3
Helixi327 – 342Combined sources16
Helixi347 – 350Combined sources4
Helixi351 – 361Combined sources11
Beta strandi364 – 368Combined sources5
Helixi372 – 374Combined sources3
Turni380 – 382Combined sources3
Beta strandi384 – 389Combined sources6
Helixi390 – 398Combined sources9
Helixi408 – 411Combined sources4
Helixi413 – 419Combined sources7
Helixi423 – 426Combined sources4
Helixi428 – 439Combined sources12
Helixi440 – 442Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HBMX-ray1.80B/E2-443[»]
1HBNX-ray1.16B/E2-443[»]
1HBOX-ray1.78B/E2-443[»]
1HBUX-ray1.90B/E2-443[»]
1MROX-ray1.16B/E2-443[»]
3M1VX-ray1.45B/E2-443[»]
3M2RX-ray1.30B/E2-443[»]
3M2UX-ray1.40B/E2-443[»]
3M2VX-ray1.80B/E2-443[»]
3M30X-ray1.45B/E2-443[»]
3M32X-ray1.35B/E2-443[»]
3POTX-ray1.20B/E1-443[»]
5A0YX-ray1.10B/E1-443[»]
5G0RX-ray1.25B/E1-443[»]
ProteinModelPortaliP11560.
SMRiP11560.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11560.

Family & Domainsi

Phylogenomic databases

eggNOGiarCOG04860. Archaea.
COG4054. LUCA.
HOGENOMiHOG000225842.
KOiK00401.
OMAiGKQMAVQ.

Family and domain databases

Gene3Di1.20.840.10. 2 hits.
3.30.70.470. 1 hit.
InterProiIPR022681. MCR_a/b_chain_a-bundle.
IPR008924. Me_CoM_Rdtase_asu/bsu_C.
IPR015823. Me_CoM_Rdtase_asu_N_sub2.
IPR003179. Me_CoM_Rdtase_bsu.
IPR022679. Me_CoM_Rdtase_bsu_C.
IPR022680. Me_CoM_Rdtase_bsu_N.
IPR009024. Me_CoM_Rdtase_Fd-like_fold.
[Graphical view]
PfamiPF02241. MCR_beta. 1 hit.
PF02783. MCR_beta_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000263. Meth_CoM_rd_beta. 1 hit.
SUPFAMiSSF48081. SSF48081. 1 hit.
SSF55088. SSF55088. 1 hit.
TIGRFAMsiTIGR03257. met_CoM_red_bet. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11560-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKFEDKVDL YDDRGNLVEE QVPLEALSPL RNPAIKSIVQ GIKRTVAVNL
60 70 80 90 100
EGIENALKTA KVGGPACKIM GRELDLDIVG NAESIAAAAK EMIQVTEDDD
110 120 130 140 150
TNVELLGGGK RALVQVPSAR FDVAAEYSAA PLVTATAFVQ AIINEFDVSM
160 170 180 190 200
YDANMVKAAV LGRYPQSVEY MGANIATMLD IPQKLEGPGY ALRNIMVNHV
210 220 230 240 250
VAATLKNTLQ AAALSTILEQ TAMFEMGDAV GAFERMHLLG LAYQGMNADN
260 270 280 290 300
LVFDLVKANG KEGTVGSVIA DLVERALEDG VIKVEKELTD YKVYGTDDLA
310 320 330 340 350
MWNAYAAAGL MAATMVNQGA ARAAQGVSST LLYYNDLIEF ETGLPSVDFG
360 370 380 390 400
KVEGTAVGFS FFSHSIYGGG GPGIFNGNHI VTRHSKGFAI PCVAAAMALD
410 420 430 440
AGTQMFSPEA TSGLIKEVFS QVDEFREPLK YVVEAAAEIK NEI
Length:443
Mass (Da):47,240
Last modified:January 23, 2007 - v3
Checksum:i1237E83E405E6D6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07794 Genomic DNA. Translation: CAA30635.1.
CP001710 Genomic DNA. Translation: ADL59131.1.
PIRiA28544.
RefSeqiWP_013296341.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL59131; ADL59131; MTBMA_c15520.
GeneIDi9705261.
KEGGimmg:MTBMA_c15520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07794 Genomic DNA. Translation: CAA30635.1.
CP001710 Genomic DNA. Translation: ADL59131.1.
PIRiA28544.
RefSeqiWP_013296341.1. NC_014408.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HBMX-ray1.80B/E2-443[»]
1HBNX-ray1.16B/E2-443[»]
1HBOX-ray1.78B/E2-443[»]
1HBUX-ray1.90B/E2-443[»]
1MROX-ray1.16B/E2-443[»]
3M1VX-ray1.45B/E2-443[»]
3M2RX-ray1.30B/E2-443[»]
3M2UX-ray1.40B/E2-443[»]
3M2VX-ray1.80B/E2-443[»]
3M30X-ray1.45B/E2-443[»]
3M32X-ray1.35B/E2-443[»]
3POTX-ray1.20B/E1-443[»]
5A0YX-ray1.10B/E1-443[»]
5G0RX-ray1.25B/E1-443[»]
ProteinModelPortaliP11560.
SMRiP11560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi79929.MTBMA_c15520.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADL59131; ADL59131; MTBMA_c15520.
GeneIDi9705261.
KEGGimmg:MTBMA_c15520.

Phylogenomic databases

eggNOGiarCOG04860. Archaea.
COG4054. LUCA.
HOGENOMiHOG000225842.
KOiK00401.
OMAiGKQMAVQ.

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.
BRENDAi2.8.4.1. 7427.

Miscellaneous databases

EvolutionaryTraceiP11560.

Family and domain databases

Gene3Di1.20.840.10. 2 hits.
3.30.70.470. 1 hit.
InterProiIPR022681. MCR_a/b_chain_a-bundle.
IPR008924. Me_CoM_Rdtase_asu/bsu_C.
IPR015823. Me_CoM_Rdtase_asu_N_sub2.
IPR003179. Me_CoM_Rdtase_bsu.
IPR022679. Me_CoM_Rdtase_bsu_C.
IPR022680. Me_CoM_Rdtase_bsu_N.
IPR009024. Me_CoM_Rdtase_Fd-like_fold.
[Graphical view]
PfamiPF02241. MCR_beta. 1 hit.
PF02783. MCR_beta_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000263. Meth_CoM_rd_beta. 1 hit.
SUPFAMiSSF48081. SSF48081. 1 hit.
SSF55088. SSF55088. 1 hit.
TIGRFAMsiTIGR03257. met_CoM_red_bet. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMCRB_METTM
AccessioniPrimary (citable) accession number: P11560
Secondary accession number(s): D9PY33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 114 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.