Q49174 (MCRX_METFV) 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
Synonyms:	mcrIIA
Ordered Locus Names:	Mfer_0734

Organism

Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S) [Complete proteome] [HAMAP]

Taxonomic identifier

523846 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanothermaceae › Methanothermus

Protein attributes

Sequence length	554 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an heterodisulfide By similarity.
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 By similarity.

Ontologies

Keywords
Biological process	Methanogenesis
Ligand	Metal-binding Nickel
Molecular function	Transferase
PTM	Methylation
Technical term	Complete 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 – 554	554	Methyl-coenzyme M reductase II subunit alpha		PRO_0000147451
Sites
	Metal binding	151	1	Nickel By similarity
Amino acid modifications
	Modified residue	261	1	Pros-methylhistidine By similarity
	Modified residue	274	1	5-methylarginine By similarity
Experimental info
	Sequence conflict	273	1	A → G in CAA50044. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q49174 [UniParc]. Last modified March 8, 2011. Version 2. Checksum: E894701807E22919	FASTA	554	61,326
	10 20 30 40 50 60 MNKKNKKLFL EALEKKFKGE SPEEKKTTFY CFGGWKQSER KREFVEYAKK LAKKRGIPFY 70 80 90 100 110 120 NPDIGVPLGQ RKLMAYRISG TDAYVEGDDL HFVNNAAIQQ MVDDIKRTVI VGMDTAHAVL 130 140 150 160 170 180 EKRLGVEVTP ETINEYMETI NHALPGGAVV QEHMVEVHPG LVDDCYAKIF TGNDELADEL 190 200 210 220 230 240 DKRVLIDINK EFPEEQAEML KKYIGNRTYQ VNRVPTIVVR CCDGGTVSRW SAMQIGMSFI 250 260 270 280 290 300 SAYKLCAGEA AIADFSFAAK HADVIEMGTI LPARRARGPN EPGGIPFGVF ADIIQTSRVS 310 320 330 340 350 360 DDPARISLEV IGAAATLYDQ VWLGSYMSGG VGFTQYASAT YTDDILDDFV YYGAEYVEDK 370 380 390 400 410 420 YGFCGVKPSM EVVKDIATEV TLYGLEQYEE YPTLLEDHFG GSQRAAVVAA AAGCSTAFAT 430 440 450 460 470 480 GNSNAGINAW YLSQILHKEG HSRLGFYGYD LQDQCGASNS LSIRSDEGLV HELRGPNYPN 490 500 510 520 530 540 YAMNVGHQPE YAGIAQAPHA ARGDAFVVNP LIKVAFADND LSFDFRWPRK EIARGALREF 550 MPDGERTLII PASK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and phylogeny of mcrII, a gene cluster encoding an isoenzyme of methyl coenzyme M reductase from hyperthermophilic Methanothermus fervidus." Lehmacher A., Klenk H.-P. Mol. Gen. Genet. 243:198-206(1994) [PubMed: 8177216] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43054 / DSM 2088 / JCM 10308 / V24 S.
[2]	"Complete genome sequence of Methanothermus fervidus type strain (V24S)." Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S., Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N. , Pati A., Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M., Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C. Stand. Genomic Sci. 3:315-324(2010) [PubMed: 21304736] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43054 / DSM 2088 / JCM 10308 / V24 S.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70765 Genomic DNA. Translation: CAA50044.1. CP002278 Genomic DNA. Translation: ADP77533.1.
PIR	S43897.
RefSeq	YP_004004295.1. NC_014658.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	9962464.
GenomeReviews	Gene locus Mfer_0734 in contig CP002278_GR.
KEGG	mfv:Mfer_0734.
Organism-specific databases
CMR	Search...
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_METFV

Accession

Primary (citable) accession number: Q49174
Secondary accession number(s): E3GZ01

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	March 8, 2011
Last modified:	January 25, 2012
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program