Reviewed, UniProtKB/Swiss-Prot Q9UXP0 (MER_METTI)

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
Synonyms:	ffdA

Organism

Methanolobus tindarius

Taxonomic identifier

2221 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanolobus

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the reversible reduction of methylene-H4MPT to methyl-H4MPT By similarity.
Catalytic activity	5-methyltetrahydromethanopterin + coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420. HAMAP MF_01091
Pathway	One-carbon metabolism; methanogenesis from carbone dioxide; methyl-CoM from 5,10-methylene-H(4)MPT: step 1/2. HAMAP MF_01091
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the mer family.

Ontologies

Keywords
Biological process	Methanogenesis One-carbon metabolism
Cellular component	Cytoplasm
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 326	326	5,10-methylenetetrahydromethanopterin reductase HAMAP MF_01091		PRO_0000084811

Sequences

	Sequence		Length	Mass (Da)
	Q9UXP0-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 16F3AB9733A45D82	FASTA	326	34,043
	10 20 30 40 50 60 MTFGIEFVPS DPVLKIAHYA KLAEQQGFDN VWITDHYNNR DVYSTLTVLA MNTNSIKLGT 70 80 90 100 110 120 GVTNPYTRNA AITASSIGSL NEISGGRAIL GLGPGEQATF DAMGISWEQP LTTTKESIAA 130 140 150 160 170 180 IRGFLAGEKV TMDGDMIKFG GAKMAFKAGD VPIYMGAQGP KMLELAGEVS DGVLINASHP 190 200 210 220 230 240 KDFEVAVKQI AAGAKKAGRD PKEVDVAAYA CFSIDKDAAK AKSAAQIVVA FIVAGSPDMV 250 260 270 280 290 300 LERHGIDPAA KADIGGAIAK GDFGALMGGM VTDSMMDAFS ICGTPDDCKA RINELLDIGV 310 320 TQIVAGSPIG PNKEKAIKLI GKEIIG

References

[1]

"The F420H2-dehydrogenase from Methanolobus tindarius: cloning of the ffd operon and expression of the genes in Escherichia coli." Westenberg D.J., Braune A., Ruppert C., Mueller V., Herzberg C., Gottschalk G., Blaut M. FEMS Microbiol. Lett. 170:389-398(1999) [PubMed: 9933933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 2278.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ011519 Genomic DNA. Translation: CAB56639.1.
PIR	T45226.
3D structure databases
HSSP	HSSP built from PDB template 1F07 based on UniProtKB Q50744.
SMR	Q9UXP0. Positions 1-326.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.99.11. 276357.
Family and domain databases
HAMAP	MF_01091. [Tree]
InterPro	IPR011251. Luciferase-like. IPR016048. Luciferase-like_sub. IPR019946. MeH4methanopterin_reductase. [Graphical view]
Gene3D	G3DSA:3.20.20.30. Luciferase_like. 1 hit.
Pfam	PF00296. Bac_luciferase. 1 hit. [Graphical view]
TIGRFAMs	TIGR03555. F420_mer. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MER_METTI

Accession

Primary (citable) accession number: Q9UXP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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