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Q49605

- MCRA_METKA

UniProt

Q49605 - MCRA_METKA

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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: 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

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi150 – 1501Nickel

GO - Molecular functioni

  1. coenzyme-B sulfoethylthiotransferase activity Source: UniProtKB-EC
  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

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
ProteomesiUP000001826: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Methyl-coenzyme M reductase I subunit alphaPRO_0000147454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601Pros-methylhistidineBy similarity
Modified residuei274 – 27415-methylarginineBy similarity

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

1
553
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 167
Helixi33 – 364
Helixi38 – 5417
Beta strandi74 – 774
Beta strandi83 – 853
Helixi86 – 883
Helixi91 – 933
Helixi95 – 10511
Beta strandi107 – 1115
Helixi113 – 1219
Helixi129 – 14214
Turni143 – 1453
Turni158 – 1603
Beta strandi165 – 1717
Helixi173 – 1764
Helixi181 – 1833
Helixi187 – 1904
Helixi193 – 20311
Beta strandi207 – 2126
Helixi215 – 2206
Helixi223 – 24220
Helixi251 – 2599
Beta strandi262 – 2665
Helixi272 – 2743
Helixi281 – 2833
Helixi286 – 2927
Helixi295 – 2984
Helixi303 – 31917
Helixi320 – 3267
Helixi334 – 3385
Helixi345 – 36016
Turni363 – 3653
Helixi370 – 39021
Helixi392 – 3976
Helixi401 – 42020
Helixi423 – 44119
Turni447 – 4504
Helixi451 – 46111
Turni465 – 4673
Helixi471 – 4733
Helixi479 – 4813
Beta strandi485 – 4873
Helixi488 – 50215
Helixi510 – 5156
Beta strandi521 – 5233
Helixi528 – 5369
Helixi547 – 5493

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6VX-ray2.70A/D1-553[»]
ProteinModelPortaliQ49605.
SMRiQ49605. Positions 8-552.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ49605.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG4058.
HOGENOMiHOG000225809.
KOiK00399.
OMAiAHSARGD.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901H → T in AAB02003. (PubMed:8863453)Curated
Sequence conflicti342 – 3421T → P in AAB02003. (PubMed:8863453)Curated
Sequence conflicti441 – 4411H → Q in AAB02003. (PubMed:8863453)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U57340 Genomic DNA. Translation: AAB02003.1.
AE009439 Genomic DNA. Translation: AAM01870.1.
RefSeqiNP_613940.1. NC_003551.1.
WP_011019025.1. NC_003551.1.

Genome annotation databases

EnsemblBacteriaiAAM01870; AAM01870; MK0655.
GeneIDi1476756.
KEGGimka:MK0655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U57340 Genomic DNA. Translation: AAB02003.1 .
AE009439 Genomic DNA. Translation: AAM01870.1 .
RefSeqi NP_613940.1. NC_003551.1.
WP_011019025.1. NC_003551.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E6V X-ray 2.70 A/D 1-553 [» ]
ProteinModelPortali Q49605.
SMRi Q49605. Positions 8-552.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 190192.MK0655.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM01870 ; AAM01870 ; MK0655 .
GeneIDi 1476756.
KEGGi mka:MK0655.

Phylogenomic databases

eggNOGi COG4058.
HOGENOMi HOG000225809.
KOi K00399.
OMAi AHSARGD.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .

Miscellaneous databases

EvolutionaryTracei Q49605.

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. "Phylogeny of Methanopyrus kandleri based on methyl coenzyme M reductase operons."
    Noelling J., Elfner A., Palmer J.R., Steigerwald V.J., Pihl T.D., Lake J.A., Reeve J.N.
    Int. J. Syst. Bacteriol. 46:1170-1173(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
  3. "Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation."
    Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U.
    J. Mol. Biol. 303:329-344(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

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: October 1, 2014
This is version 105 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

External Data

Dasty 3