A9SS00 (MTND2_PHYPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2
EC=1.13.11.54

Alternative name(s):
Acireductone dioxygenase (Fe(2+)-requiring) 2
Short name=ARD 2
Short name=Fe-ARD 2

Gene names

ORF Names:

PHYPADRAFT_134384

Organism

Physcomitrella patens subsp. patens (Moss) [Reference proteome]

Taxonomic identifier

145481 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Bryophyta › Bryophytina › Bryopsida › Funariidae › Funariales › Funariaceae › Physcomitrella › Physcomitrella patens

Protein attributes

Sequence length	195 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) By similarity. HAMAP-Rule MF_03154
Catalytic activity	1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate. HAMAP-Rule MF_03154
Cofactor	Binds 1 iron ion per monomer. Can also use other divalent metal cations By similarity.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6. HAMAP-Rule MF_03154
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the acireductone dioxygenase (ARD) family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-methionine salvage from methylthioadenosine Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acireductone dioxygenase [iron(II)-requiring] 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 – 195	195	1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase 2 HAMAP-Rule MF_03154		PRO_0000414343
Sites
	Metal binding	94	1	Iron or nickel By similarity
	Metal binding	96	1	Iron or nickel By similarity
	Metal binding	100	1	Iron or nickel By similarity
	Metal binding	139	1	Iron or nickel By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9SS00 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: D0AED4C8E9A82C70	FASTA	195	23,199
	10 20 30 40 50 60 MQVQRPPLEA WYMNDSEEDQ RLPHHRNPPE YVTLEKLAAL GVIHWVLDAD NHETDPELSI 70 80 90 100 110 120 IRKDRGYNYT DVITVCPEML PSYEAKIKSF YEEHIHMDEE IRYCLDGSGY FDVRDPEDHW 130 140 150 160 170 180 IRIWVRKGDM IVLPAGCYHR FTLDEHNYIM AMRLFVGEPI WTPYNRPQDE HPVRKGYVHQ 190 FLQPELLDVD MSISA

References

[1]

"The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants." Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., Suzuki Y. , Hashimoto S.-I., Yamaguchi K., Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L. Science 319:64-69(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Gransden 2004.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS545000 Genomic DNA. Translation: EDQ66042.1.
RefSeq	XP_001769170.1. XM_001769118.1.
3D structure databases
ProteinModelPortal	A9SS00.
SMR	A9SS00. Positions 8-178.
ModBase	Search...
Protein-protein interaction databases
STRING	3218.JGI134384.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5932378.
KEGG	ppp:PHYPADRAFT_134384.
Phylogenomic databases
KO	K08967.
ProtClustDB	CLSN2683301.
Enzyme and pathway databases
UniPathway	UPA00904; UER00878.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
HAMAP	MF_03154. Salvage_MtnD_euk.
InterPro	IPR004313. Acireductn_dOase_family. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR23418. PTHR23418. 1 hit.
Pfam	PF03079. ARD. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTND2_PHYPA

Accession

Primary (citable) accession number: A9SS00

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 14, 2011
Last sequence update:	February 5, 2008
Last modified:	April 3, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program