P21110 (MCRX_METTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methyl-coenzyme M reductase II subunit alpha
Short name=MCR II alpha
EC=2.8.4.1

Alternative name(s):
Coenzyme-B sulfoethylthiotransferase alpha

Gene names

Name:	mrtA
Ordered Locus Names:	MTH_1129

Organism

Methanobacterium thermoautotrophicum (strain Delta H)

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an heterodisulfide.
Catalytic activity	Methyl-CoM + CoB = CoM-S-S-CoB + methane.
Cofactor	Binds 2 coenzyme F430 noncovalently per hexamer. Coenzyme F430 is a yellow nickel porphinoid By similarity.
Pathway	One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1.
Subunit structure	Hexamer of two alpha, two beta, and two gamma chains.
Developmental stage	There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contains mostly MCR I.

Ontologies

Keywords
Biological process	Methanogenesis
Ligand	Metal-binding Nickel
Molecular function	Transferase
PTM	Methylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	coenzyme-B sulfoethylthiotransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 553	553	Methyl-coenzyme M reductase II subunit alpha		PRO_0000147457
Sites
	Metal binding	150	1	Nickel By similarity
Amino acid modifications
	Modified residue	260	1	Pros-methylhistidine By similarity
	Modified residue	273	1	5-methylarginine By similarity
Experimental info
	Sequence conflict	6	1	L → H in AAA73439. Ref.1
	Sequence conflict	24	1	Y → I in AAA73439. Ref.1
	Sequence conflict	168	1	I → V in AAA73439. Ref.1
	Sequence conflict	200	1	K → KEQLK Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21110 [UniParc]. Last modified May 30, 2000. Version 3. Checksum: 8A3511715F7EFE00	FASTA	553	60,707
	10 20 30 40 50 60 MDEKKLFLTA LKKKFEVEDP DEKYTNFYCF GGWEQSARKK EFTEYAKKAA EKRGGIPFYN 70 80 90 100 110 120 PDIGVPLGQR KLMAYRVSGT DAYVEGDDLH FVNNAAIQQM VDDIKRTVIV GMDTAHAVLE 130 140 150 160 170 180 KRLGVEVTPE TINEYMEAIN HALPGGAVVQ EHMVEVHPGL VEDCYAKIFT GDDNLADELD 190 200 210 220 230 240 KRILIDINKE FPEEQAEQLK SYIGNRTYQV NRVPTIVVRT CDGGTVSRWS AMQIGMSFIS 250 260 270 280 290 300 AYKLCAGEAA IADFSYAAKH ADVIEMGTIM PARRARGPNE PGGVAFGTFA DIVQASRVSD 310 320 330 340 350 360 DPAKISLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY YGMEYVDDKY 370 380 390 400 410 420 GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG SQRAAVAAAA AGCSTAFATG 430 440 450 460 470 480 NSNAGINGWY LSQILHKEAH SRLGFYGYDL QDQCGASNSL SIRSDEGLIH ELRGPNYPNY 490 500 510 520 530 540 AMNVGHQPEY AGIAQAPHAA RGDAFCTNPL IKVAFADKDL SFDFTSPRKS IAAGALREFM 550 PEGERDLIIP AGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7929010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Delta H.
[2]	"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 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: 2269306] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. Strain: Delta H.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09990 Genomic DNA. Translation: AAA73439.1. AE000666 Genomic DNA. Translation: AAB85618.1.
PIR	C69017. T45150.
RefSeq	NP_276257.1. NC_000916.1.
3D structure databases
ProteinModelPortal	P21110.
SMR	P21110. Positions 6-551.
ModBase	Search...
Protein-protein interaction databases
IntAct	P21110. 2 interactions.
STRING	P21110.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1471537.
GenomeReviews	Gene locus MTH_1129 in contig AE000666_GR.
KEGG	mth:MTH1129.
NMPDR	fig|187420.1.peg.1112.
Phylogenomic databases
eggNOG	arNOG04802.
HOGENOM	HBG541009.
OMA	QPEYAGI.
ProtClustDB	CLSK876061.
Enzyme and pathway databases
BioCyc	MetaCyc:MRTAMAUTO-MONOMER. MTHE187420:MTH1129-MONOMER.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:1.20.840.10. MCR_a/b_chain_a-bundle. 1 hit. G3DSA:3.90.390.10. Me_CoM_Rdtase_asu_N_sub1. 1 hit. G3DSA:3.30.70.470. Me_CoM_Rdtase_asu_N_sub2. 1 hit.
KO	K00399.
Pfam	PF02249. MCR_alpha. 1 hit. PF02745. MCR_alpha_N. 1 hit. [Graphical view]
PIRSF	PIRSF000262. MCR_alpha. 1 hit.
SUPFAM	SSF48081. MCR_alpha_beta_C. 1 hit. SSF55088. MCR_fer_like. 1 hit.
TIGRFAMs	TIGR03256. Met_CoM_red_alp. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MCRX_METTH

Accession

Primary (citable) accession number: P21110
Secondary accession number(s): O27201, Q50487

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program