Q50744 (MER_METTM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5,10-methylenetetrahydromethanopterin reductase
EC=1.5.99.11

Alternative name(s):
Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase
Methylene-H(4)MPT reductase

Gene names

Name:	mer
Ordered Locus Names:	MTBMA_c03270

Organism

Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP]

Taxonomic identifier

79929 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible reduction of methylene-H4MPT to methyl-H4MPT. HAMAP MF_01091
Catalytic activity	5-methyltetrahydromethanopterin + coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420. HAMAP MF_01091
Pathway	One-carbon metabolism; methanogenesis from CO(2); methyl-coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step 1/2. HAMAP MF_01091
Subunit structure	Homotetramer Probable.
Subcellular location	Cytoplasm HAMAP MF_01091.
Sequence similarities	Belongs to the mer family.

Ontologies

Keywords
Biological process	Methanogenesis One-carbon metabolism
Cellular component	Cytoplasm
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 321

321

5,10-methylenetetrahydromethanopterin reductase HAMAP MF_01091

PRO_0000084812

Experimental info

Sequence conflict

15

1

K → W AA sequence Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

321

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Beta strand

9 – 11

3

Helix

13 – 25

13

Beta strand

30 – 33

4

Helix

42 – 51

10

Beta strand

57 – 63

7

Beta strand

65 – 68

4

Helix

70 – 83

14

Beta strand

90 – 92

3

Helix

97 – 102

6

Helix

110 – 125

16

Beta strand

142 – 145

4

Beta strand

148 – 151

4

Helix

155 – 164

10

Beta strand

166 – 170

5

Helix

175 – 191

17

Helix

196 – 198

3

Beta strand

199 – 209

11

Helix

213 – 229

17

Helix

233 – 238

6

Helix

245 – 253

9

Turn

254 – 256

3

Helix

258 – 263

6

Helix

267 – 273

7

Beta strand

275 – 277

3

Helix

279 – 291

13

Beta strand

296 – 303

8

Helix

307 – 319

13

Sequences

	Sequence		Length	Mass (Da)
	Q50744 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 473DB8BD37486D43	FASTA	321	33,488
	10 20 30 40 50 60 MKFGIEFVPN EPIEKIVKLV KLAEDVGFEY AWITDHYNNK NVYETLALIA EGTETIKLGP 70 80 90 100 110 120 GVTNPYVRSP AITASAIATL DELSNGRATL GIGPGDKATF DALGIEWVKP VSTIRDAIAM 130 140 150 160 170 180 MRTLLAGEKT ESGAQLMGVK AVQEKIPIYM GAQGPMMLKT AGEISDGALI NASNPKDFEA 190 200 210 220 230 240 AVPLIKEGAE AAGKSIADID VAAYTCCSID EDAAAAANAA KIVVAFIAAG SPPPVFERHG 250 260 270 280 290 300 LPADTGKKFG ELLGKGDFGG AIGAVDDALM EAFSVVGTPD EFIPKIEALG EMGVTQYVAG 310 320 SPIGPDKEKS IKLLGEVIAS F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin reductase (Mer) from Methanobacterium thermoautotrophicum strain Marburg -- cloning, sequencing, transcriptional analysis, and functional expression in Escherichia coli of the mer gene." Vaupel M., Thauer R.K. Eur. J. Biochem. 231:773-778(1995) [PubMed: 7649177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[2]	"Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism." Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K. J. Bacteriol. 192:5850-5851(2010) [PubMed: 20802048] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[3]	"Purification and properties of N5,N10-methylenetetrahydromethanopterin reductase (coenzyme F420-dependent) from the extreme thermophile Methanopyrus kandleri." Ma K., Linder D., Stetter K.O., Thauer R.K. Arch. Microbiol. 155:593-600(1991) [PubMed: 1953299] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-31. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[4]	"Purification and properties of N5, N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg)." Ma K., Thauer R.K. Eur. J. Biochem. 191:187-193(1990) [PubMed: 2379499] [Abstract] Cited for: CHARACTERIZATION. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[5]	"Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea." Shima S., Warkentin E., Grabarse W., Sordel M., Wicke M., Thauer R.K., Ermler U. J. Mol. Biol. 300:935-950(2000) [PubMed: 10891279] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X86477 Genomic DNA. Translation: CAA60203.1.
CP001710 Genomic DNA. Translation: ADL57933.1.

PIR

S66529.

RefSeq

YP_003849246.1. NC_014408.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F07	X-ray	2.00	A/B/C/D	1-321	[»]

ProteinModelPortal

Q50744.

SMR

Q50744. Positions 1-321.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

9704033.

GenomeReviews

Gene locus MTBMA_c03270 in contig CP001710_GR.

KEGG

mmg:MTBMA_c03270.

Organism-specific databases

CMR

Search...

Phylogenomic databases

OMA

GIEFVPG.

ProtClustDB

PRK02271.

Family and domain databases

HAMAP

MF_01091. F420_mer.
[Tree]

InterPro

IPR011251. Luciferase-like_dom.
IPR019946. MeH4methanopterin_reductase.
[Graphical view]

Gene3D

G3DSA:3.20.20.30. Luciferase_like. 1 hit.

KO

K00320.

Pfam

PF00296. Bac_luciferase. 1 hit.
[Graphical view]

SUPFAM

SSF51679. Luciferase_like. 1 hit.

TIGRFAMs

TIGR03555. F420_mer. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MER_METTM

Accession

Primary (citable) accession number: Q50744
Secondary accession number(s): D9PUN5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	November 1, 1996
Last modified:	November 16, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program