Reviewed, UniProtKB/Swiss-Prot Q1W377 (PMM_SOLLC)

Names and origin

Protein names	Recommended name:     Phosphomannomutase     EC=5.4.2.8 Alternative name(s):     LePMM
Organism	Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier	4081 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in ascorbic acid biosynthesis and in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions By similarity.
Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Pathway	Nucleotide-sugar biosynthesis; GDP-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the eukaryotic PMM family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase
Gene Ontology (GO)
Biological process	mannose biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphomannomutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 252	252	Phosphomannomutase		PRO_0000326494

Sequences

	Sequence		Length	Mass (Da)
	Q1W377-1 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: AE3E701AC82DCC82	FASTA	252	28,556
	10 20 30 40 50 60 MAARKAGLIA LFDVDGTLTA PRKESTPQML KFMQELRKVV TVGVVGGSDL VKISEQLGNT 70 80 90 100 110 120 VTNDYDYVFS ENGLVAHKDG KLIGKQSLKS HLGDEKLKEF INFTLHYIAD LDIPIKRGTF 130 140 150 160 170 180 IEFRSGMLNV SPIGRNCSQE ERDEFEKYDK VQKIRETMVS VLREKFAHFN LTFSIGGQIS 190 200 210 220 230 240 FDVFPQGWDK TYCLRYLEEF NEIHFFGDKT YKGGNDHEIY ESERTVGHTV TSPEETLKQC 250 SVLFLGKDNG SS

References

[1]

"Molecular and functional analysis of phosphomannomutase (PMM) from higher plants and genetic evidence for the involvement of PMM in ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana." Qian W., Yu C., Qin H., Liu X., Zhang A., Johansen I.E., Wang D. Plant J. 49:399-413(2007) [PubMed: 17217471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ442993 mRNA. Translation: ABD97872.1.
UniGene	Les.5106
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.4.2.8. 281054.
Family and domain databases
InterPro	IPR006379. HAD-SF_hydro_IIB. IPR005002. PMM. [Graphical view]
PANTHER	PTHR10466. PMM. 1 hit.
Pfam	PF03332. PMM. 1 hit. [Graphical view]
TIGRFAMs	TIGR01484. HAD-SF-IIB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PMM_SOLLC

Accession

Primary (citable) accession number: Q1W377

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 2, 2006
Last modified:	June 16, 2009
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)