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Protein

Methyl-coenzyme M reductase I subunit alpha

Gene

mcrA

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed-Annotation score: Annotation score: 4 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 I subunit alpha (mcrA)
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 bindingi150Nickel1

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

BRENDAi2.8.4.1. 3274.
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:MK0655
OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifieri190192 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
Proteomesi
  • UP000001826 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001474541 – 553Methyl-coenzyme M reductase I subunit alphaAdd BLAST553

Amino acid modifications

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

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi190192.MK0655.

Structurei

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 16Combined sources7
Helixi33 – 36Combined sources4
Helixi38 – 54Combined sources17
Beta strandi74 – 77Combined sources4
Beta strandi83 – 85Combined sources3
Helixi86 – 88Combined sources3
Helixi91 – 93Combined sources3
Helixi95 – 105Combined sources11
Beta strandi107 – 111Combined sources5
Helixi113 – 121Combined sources9
Helixi129 – 142Combined sources14
Turni143 – 145Combined sources3
Turni158 – 160Combined sources3
Beta strandi165 – 171Combined sources7
Helixi173 – 176Combined sources4
Helixi181 – 183Combined sources3
Helixi187 – 190Combined sources4
Helixi193 – 203Combined sources11
Beta strandi207 – 212Combined sources6
Helixi215 – 220Combined sources6
Helixi223 – 242Combined sources20
Helixi251 – 259Combined sources9
Beta strandi262 – 266Combined sources5
Helixi272 – 274Combined sources3
Helixi281 – 283Combined sources3
Helixi286 – 292Combined sources7
Helixi295 – 298Combined sources4
Helixi303 – 319Combined sources17
Helixi320 – 326Combined sources7
Helixi334 – 338Combined sources5
Helixi345 – 360Combined sources16
Turni363 – 365Combined sources3
Helixi370 – 390Combined sources21
Helixi392 – 397Combined sources6
Helixi401 – 420Combined sources20
Helixi423 – 441Combined sources19
Turni447 – 450Combined sources4
Helixi451 – 461Combined sources11
Turni465 – 467Combined sources3
Helixi471 – 473Combined sources3
Helixi479 – 481Combined sources3
Beta strandi485 – 487Combined sources3
Helixi488 – 502Combined sources15
Helixi510 – 515Combined sources6
Beta strandi521 – 523Combined sources3
Helixi528 – 536Combined sources9
Helixi547 – 549Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E6VX-ray2.70A/D1-553[»]
ProteinModelPortaliQ49605.
SMRiQ49605.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ49605.

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.

Q49605-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAEEKLFM KALKEKFEES PEEKYTKFYI FGGWKQSERK KEFKEWADKI
60 70 80 90 100
VEERGVPHYN PDIGVPLGQR KLMSYQVSGT DVFVEGDDLH FVNNAAMQQM
110 120 130 140 150
WDDIRRTVIV GMDTAHRVLE RRLGKEVTPE TINEYMETLN HALPGGAVVQ
160 170 180 190 200
EHMVEIHPGL TWDCYAKIIT GDLELADEID DKFLIDIEKL FPEEQAEQLI
210 220 230 240 250
KAIGNRTYQV CRMPTIVGHV CDGATMYRWA AMQIAMSFIC AYKIAAGEAA
260 270 280 290 300
VSDFAFASKH AEVINMGEML PARRARGENE PGGVPFGVLA DCVQTMRKYP
310 320 330 340 350
DDPAKVALEV IAAGAMLYDQ IWLGSYMSGG VGFTQYATAV YTDNILDDYV
360 370 380 390 400
YYGLEYVEDK YGIAEAEPSM DVVKDVATEV TLYGLEQYER YPAAMETHFG
410 420 430 440 450
GSQRAAVCAA AAGCSTAFAT GHAQAGLNGW YLSQILHKEG HGRLGFYGYA
460 470 480 490 500
LQDQCGAANS LSVRSDEGLP LELRGPNYPN YAMNVGHLGE YAGIVQAAHA
510 520 530 540 550
ARGDAFCVHP VIKVAFADEN LVFDFTEPRK EFAKGALREF EPAGERDLIV

PAE
Length:553
Mass (Da):61,384
Last modified:April 16, 2002 - v2
Checksum:iF26582E0DCF2A434
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti90H → T in AAB02003 (PubMed:8863453).Curated1
Sequence conflicti342T → P in AAB02003 (PubMed:8863453).Curated1
Sequence conflicti441H → Q in AAB02003 (PubMed:8863453).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57340 Genomic DNA. Translation: AAB02003.1.
AE009439 Genomic DNA. Translation: AAM01870.1.

Genome annotation databases

EnsemblBacteriaiAAM01870; AAM01870; MK0655.
KEGGimka:MK0655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57340 Genomic DNA. Translation: AAB02003.1.
AE009439 Genomic DNA. Translation: AAM01870.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E6VX-ray2.70A/D1-553[»]
ProteinModelPortaliQ49605.
SMRiQ49605.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190192.MK0655.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM01870; AAM01870; MK0655.
KEGGimka:MK0655.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.
BRENDAi2.8.4.1. 3274.

Miscellaneous databases

EvolutionaryTraceiQ49605.

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_METKA
AccessioniPrimary (citable) accession number: Q49605
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 16, 2002
Last modified: November 2, 2016
This is version 118 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, Reference proteome

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.