Q49605 (MCRA_METKA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Coenzyme-B sulfoethylthiotransferase alpha

Gene names

Name:	mcrA
Ordered Locus Names:	MK0655

Organism

Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)

Taxonomic identifier

190192 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

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.

Ontologies

Keywords
Biological process	Methanogenesis
Ligand	Metal-binding Nickel
Molecular function	Transferase
PTM	Methylation
Technical term	3D-structure 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 – 553

553

Methyl-coenzyme M reductase I subunit alpha

PRO_0000147454

Sites

Metal binding

150

1

Nickel

Amino acid modifications

Modified residue

260

1

Pros-methylhistidine By similarity

Modified residue

273

1

5-methylarginine By similarity

Experimental info

Sequence conflict

90

1

H → T in AAB02003. Ref.1

Sequence conflict

342

1

T → P in AAB02003. Ref.1

Sequence conflict

441

1

H → Q in AAB02003. Ref.1

Secondary structure

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553

Helix Strand Turn

Details...

Helix

10 – 16

7

Helix

33 – 36

4

Helix

38 – 54

17

Beta strand

74 – 77

4

Beta strand

83 – 85

3

Helix

86 – 88

3

Helix

91 – 93

3

Helix

95 – 105

11

Beta strand

107 – 111

5

Helix

113 – 121

9

Helix

129 – 142

14

Turn

143 – 145

3

Turn

158 – 160

3

Beta strand

165 – 171

7

Helix

173 – 176

4

Helix

181 – 183

3

Helix

187 – 190

4

Helix

193 – 203

11

Beta strand

207 – 212

6

Helix

215 – 220

6

Helix

223 – 242

20

Helix

251 – 259

9

Beta strand

262 – 266

5

Helix

272 – 274

3

Helix

281 – 283

3

Helix

286 – 292

7

Helix

295 – 298

4

Helix

303 – 319

17

Helix

320 – 326

7

Helix

334 – 338

5

Helix

345 – 360

16

Turn

363 – 365

3

Helix

370 – 390

21

Helix

392 – 397

6

Helix

401 – 420

20

Helix

423 – 441

19

Turn

447 – 450

4

Helix

451 – 461

11

Turn

465 – 467

3

Helix

471 – 473

3

Helix

479 – 481

3

Beta strand

485 – 487

3

Helix

488 – 502

15

Helix

510 – 515

6

Beta strand

521 – 523

3

Helix

528 – 536

9

Helix

547 – 549

3

Sequences

	Sequence		Length	Mass (Da)
	Q49605 [UniParc]. Last modified April 16, 2002. Version 2. Checksum: F26582E0DCF2A434	FASTA	553	61,384
	10 20 30 40 50 60 MSSAEEKLFM KALKEKFEES PEEKYTKFYI FGGWKQSERK KEFKEWADKI VEERGVPHYN 70 80 90 100 110 120 PDIGVPLGQR KLMSYQVSGT DVFVEGDDLH FVNNAAMQQM WDDIRRTVIV GMDTAHRVLE 130 140 150 160 170 180 RRLGKEVTPE TINEYMETLN HALPGGAVVQ EHMVEIHPGL TWDCYAKIIT GDLELADEID 190 200 210 220 230 240 DKFLIDIEKL FPEEQAEQLI KAIGNRTYQV CRMPTIVGHV CDGATMYRWA AMQIAMSFIC 250 260 270 280 290 300 AYKIAAGEAA VSDFAFASKH AEVINMGEML PARRARGENE PGGVPFGVLA DCVQTMRKYP 310 320 330 340 350 360 DDPAKVALEV IAAGAMLYDQ IWLGSYMSGG VGFTQYATAV YTDNILDDYV YYGLEYVEDK 370 380 390 400 410 420 YGIAEAEPSM DVVKDVATEV TLYGLEQYER YPAAMETHFG GSQRAAVCAA AAGCSTAFAT 430 440 450 460 470 480 GHAQAGLNGW YLSQILHKEG HGRLGFYGYA LQDQCGAANS LSVRSDEGLP LELRGPNYPN 490 500 510 520 530 540 YAMNVGHLGE YAGIVQAAHA ARGDAFCVHP VIKVAFADEN LVFDFTEPRK EFAKGALREF 550 EPAGERDLIV PAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phylogeny of Methanopyrus kandleri based on methyl coenzyme M reductase operons." Noelling J., Elfner A., Palmer J.R., Steigerwald V.J., Pihl T.D., Lake J.A., Reeve J.N. Int. J. Syst. Bacteriol. 46:1170-1173(1996) [PubMed: 8863453] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[3]	"Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation." Grabarse W., Mahlert F., Shima S., Thauer R.K., Ermler U. J. Mol. Biol. 303:329-344(2000) [PubMed: 11023796] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U57340 Genomic DNA. Translation: AAB02003.1.
AE009439 Genomic DNA. Translation: AAM01870.1.

RefSeq

NP_613940.1. NC_003551.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E6V	X-ray	2.70	A/D	1-553	[»]

ProteinModelPortal

Q49605.

SMR

Q49605. Positions 8-552.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1476756.

GenomeReviews

Gene locus MK0655 in contig AE009439_GR.

KEGG

mka:MK0655.

NMPDR

fig|190192.1.peg.653.

Phylogenomic databases

HOGENOM

HBG541009.

OMA

QPEYAGI.

ProtClustDB

CLSK876061.

Enzyme and pathway databases

BioCyc

MKAN190192:MK0655-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

MCRA_METKA

Accession

Primary (citable) accession number: Q49605

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	April 16, 2002
Last modified:	January 25, 2012
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program