Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q49605

- MCRA_METKA

UniProt

Q49605 - MCRA_METKA

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    MSSAEEKLFM KALKEKFEES PEEKYTKFYI FGGWKQSERK KEFKEWADKI    50
    VEERGVPHYN PDIGVPLGQR KLMSYQVSGT DVFVEGDDLH FVNNAAMQQM 100
    WDDIRRTVIV GMDTAHRVLE RRLGKEVTPE TINEYMETLN HALPGGAVVQ 150
    EHMVEIHPGL TWDCYAKIIT GDLELADEID DKFLIDIEKL FPEEQAEQLI 200
    KAIGNRTYQV CRMPTIVGHV CDGATMYRWA AMQIAMSFIC AYKIAAGEAA 250
    VSDFAFASKH AEVINMGEML PARRARGENE PGGVPFGVLA DCVQTMRKYP 300
    DDPAKVALEV IAAGAMLYDQ IWLGSYMSGG VGFTQYATAV YTDNILDDYV 350
    YYGLEYVEDK YGIAEAEPSM DVVKDVATEV TLYGLEQYER YPAAMETHFG 400
    GSQRAAVCAA AAGCSTAFAT GHAQAGLNGW YLSQILHKEG HGRLGFYGYA 450
    LQDQCGAANS LSVRSDEGLP LELRGPNYPN YAMNVGHLGE YAGIVQAAHA 500
    ARGDAFCVHP VIKVAFADEN LVFDFTEPRK EFAKGALREF EPAGERDLIV 550
    PAE 553
    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

    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