Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P21110

- MCRX_METTH

UniProt

P21110 - MCRX_METTH

(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)

Protein

Methyl-coenzyme M reductase II subunit alpha

Gene

mrtA

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed - 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 F430By similarityNote: Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme F430 is a yellow nickel porphinoid.By similarity

Pathwayi

Sites

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

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

BioCyciMetaCyc:MRTAMAUTO-MONOMER.
MTHE187420:GJNM-1131-MONOMER.
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
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase alpha
Gene namesi
Name:mrtA
Ordered Locus Names:MTH_1129
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000005223: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Methyl-coenzyme M reductase II subunit alphaPRO_0000147457Add
BLAST

Amino acid modifications

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

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

IntActiP21110. 2 interactions.
STRINGi187420.MTH1129.

Structurei

3D structure databases

ProteinModelPortaliP21110.
SMRiP21110. Positions 6-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG4058.
KOiK00399.
OMAiGHQPEYA.

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.

P21110-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDEKKLFLTA LKKKFEVEDP 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 DIVQASRVSD
310 320 330 340 350
DPAKISLEVI 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 SFDFTSPRKS IAAGALREFM PEGERDLIIP

AGK
Length:553
Mass (Da):60,707
Last modified:May 30, 2000 - v3
Checksum:i8A3511715F7EFE00
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61L → H in AAA73439. (PubMed:7929010)Curated
Sequence conflicti24 – 241Y → I in AAA73439. (PubMed:7929010)Curated
Sequence conflicti168 – 1681I → V in AAA73439. (PubMed:7929010)Curated
Sequence conflicti200 – 2001K → KEQLK(PubMed:7929010)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09990 Genomic DNA. Translation: AAA73439.1.
AE000666 Genomic DNA. Translation: AAB85618.1.
PIRiC69017.
T45150.
RefSeqiNP_276257.1. NC_000916.1.
WP_010876753.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85618; AAB85618; MTH_1129.
GeneIDi1471537.
KEGGimth:MTH1129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09990 Genomic DNA. Translation: AAA73439.1 .
AE000666 Genomic DNA. Translation: AAB85618.1 .
PIRi C69017.
T45150.
RefSeqi NP_276257.1. NC_000916.1.
WP_010876753.1. NC_000916.1.

3D structure databases

ProteinModelPortali P21110.
SMRi P21110. Positions 6-551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P21110. 2 interactions.
STRINGi 187420.MTH1129.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB85618 ; AAB85618 ; MTH_1129 .
GeneIDi 1471537.
KEGGi mth:MTH1129.

Phylogenomic databases

eggNOGi COG4058.
KOi K00399.
OMAi GHQPEYA.

Enzyme and pathway databases

UniPathwayi UPA00646 ; UER00699 .
BioCyci MetaCyc:MRTAMAUTO-MONOMER.
MTHE187420:GJNM-1131-MONOMER.

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. "Growth phase-dependent transcription of the genes that encode the two methyl coenzyme M reductase isoenzymes and N5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum delta H."
    Pihl T.D., Sharma S., Reeve J.N.
    J. Bacteriol. 176:6384-6391(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  3. "Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H."
    Rospert S., Linder D., Ellermann J., Thauer R.K.
    Eur. J. Biochem. 194:871-877(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-15.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Entry informationi

Entry nameiMCRX_METTH
AccessioniPrimary (citable) accession number: P21110
Secondary accession number(s): O27201, Q50487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 30, 2000
Last modified: November 26, 2014
This is version 108 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3