Reviewed, UniProtKB/Swiss-Prot O27232 (MCRA_METTH)

Names and origin

Protein names

Recommended name:
    Methyl-coenzyme M reductase subunit alpha
    EC=2.8.4.1
Alternative name(s):
    Coenzyme-B sulfoethylthiotransferase alpha

Gene names

Name:	mcrA
Ordered Locus Names:	MTH_1164

Organism

Methanobacterium thermoautotrophicum [Complete proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = 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-CoM reduction; methane from methyl-CoM: 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
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 nickel 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
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 550	549	Methyl-coenzyme M reductase subunit alpha		PRO_0000147455
Sites
	Metal binding	147	1	Nickel By similarity
Amino acid modifications
	Modified residue	257	1	Pros-methylhistidine By similarity
	Modified residue	270	1	5-methylarginine By similarity
Experimental info
	Sequence conflict	288	1	D → E in AAA73445. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O27232-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DE8184A3A79468CC	FASTA	550	60,482
	10 20 30 40 50 60 MADKLFINAL KKKFEESPEE KKTTFYTLGG WKQSERKTEF VNAGKEVAAK RGIPQYNPDI 70 80 90 100 110 120 GTPLGQRVLM PYQVSTTDTF VEGDDLHFVN NAAMQQMWDD IRRTVIVGLN HAHAVIEKRL 130 140 150 160 170 180 GKEVTPETIT HYLETVNHAM PGAAVVQEHM VETHPALVAD SYVKVFTGND EIADEIDPAF 190 200 210 220 230 240 VIDINKQFPE DQAETLKAEV GDGIWQVVRI PTIVSRTCDG ATTSRWSAMQ IGMSMISAYK 250 260 270 280 290 300 QAAGEAATGD FAYAAKHAEV IHMGTYLPVR RARGENEPGG VPFGYLADIC QSSRVNYEDP 310 320 330 340 350 360 VRVSLDVVAT GAMLYDQIWL GSYMSGGVGF TQYATAAYTD NILDDFTYFG KEYVEDKYGL 370 380 390 400 410 420 CEAPNTMDTV LDVASEVTFY GLEQYEEYPA LLEDQFGGSQ RAAVVAAAAG CSTAFATANA 430 440 450 460 470 480 QTGLSGWYLS MYLHKEQHSR LGFYGYDLQD QCGASNVFSI RGDEGLPLEL RGPNYPNYAM 490 500 510 520 530 540 NVGHQGEYAG ISQAPHAARG DAFVFNPLVK IAFADDNLVF DFTNVRGEFA KGALREFEPA 550 GERALITPAK

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 2-19. Strain: Delta H.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U10036 Genomic DNA. Translation: AAA73445.1. AE000666 Genomic DNA. Translation: AAB85653.1.
PIR	B69022.
RefSeq	NP_276292.1.
3D structure databases
HSSP	HSSP built from PDB template 1HBN based on UniProtKB P11558.
SMR	O27232. Positions 2-549.
ModBase	Search...
Genome annotation databases
GeneID	1471572.
GenomeReviews	Gene locus MTH_1164 in contig AE000666_GR.
KEGG	mth:MTH1164.
NMPDR	fig|187420.1.peg.1147.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O27232.
OMA	O27232. MSMISAY.
Enzyme and pathway databases
BioCyc	MTHE187420:MTH1164-MON.
BRENDA	2.8.4.1. 270.
Family and domain databases
InterPro	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. [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.
Pfam	PF02249. MCR_alpha. 1 hit. PF02745. MCR_alpha_N. 1 hit. [Graphical view]
PIRSF	PIRSF000262. MCR_alpha. 1 hit.
TIGRFAMs	TIGR03256. met_CoM_red_alp. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MCRA_METTH

Accession

Primary (citable) accession number: O27232
Secondary accession number(s): Q50493

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)