Q60391 (MCRX_METJA) 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:	mtrA
Ordered Locus Names:	MJ0083

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	552 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.
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 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 – 552	552	Methyl-coenzyme M reductase II subunit alpha		PRO_0000147453
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

Sequences

	Sequence		Length	Mass (Da)
	Q60391 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: DB66781796B987CE	FASTA	552	61,241
	10 20 30 40 50 60 MDVEKKLFLK ALKEKFEEDP KEKYTKFYIF GGWRQSARKR EFVEFAQKLI EKRGGIPFYN 70 80 90 100 110 120 PDIGVPLGQR KLMTYKISGT DAFVEGDDLH FCNNAAIQQL VDDIKRTVIV GMDTAHAVLE 130 140 150 160 170 180 KRLGVEVTPE TINEYMETIN HALPGGAVVQ EHMVEVHPGL VWDCYAKIFT GNDELADEID 190 200 210 220 230 240 KRFLIDINKE FPEEQAEQIK KYIGNRTYQV SRVPTIVVRC CDGGTVSRWS AMQIGMSFIT 250 260 270 280 290 300 AYKLCAGEAA IADFSYAAKH ADVIQMGMIL PARRARGPNE PGGVPFGIFA DIIQTSRVSD 310 320 330 340 350 360 DPAQVTLEVI GAAATFYDQV WLGSYMSGGV GFTQYASATY TDDILDDFVY YGMDYVEKKY 370 380 390 400 410 420 GLCGVKPSME VVKDIATEVT LYGLEQYDEY PALLEDHFGG SQRAGVTAAA AGCSVAFATG 430 440 450 460 470 480 NSNAGINGWY LSQILHKEYH SRLGFYGYDL QDQCGAANSL SIRSDEGLLH ECRGPNYPNY 490 500 510 520 530 540 AMNVGHQPEY AGIAQAPHAA RGDAFCLNPI IKVAFADDNL IFDFKWPRKC IAKGALREFE 550 PAGERDLIIP AA

References

[1]

"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB98063.1.
PIR	C64310.
RefSeq	NP_247047.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q60391.
SMR	Q60391. Positions 7-551.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1450922.
GenomeReviews	Gene locus MJ0083 in contig L77117_GR.
KEGG	mja:MJ_0083.
NMPDR	fig|243232.1.peg.84.
TIGR	MJ0083.
Phylogenomic databases
HOGENOM	HBG541009.
OMA	QPEYAGI.
ProtClustDB	CLSK876061.
Enzyme and pathway databases
BioCyc	MJAN243232:MJ_0083-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_METJA

Accession

Primary (citable) accession number: Q60391

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program