O80840 (PMM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphomannomutase
Short name=AtPMM
EC=5.4.2.8

Gene names

Name:	PMM
Ordered Locus Names:	At2g45790
ORF Names:	F4I18.23

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Ref.1 Ref.6
Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in roots, stems, leaves, flower buds, flowers and immature fruits. Ref.1
Disruption phenotype	The thermosensitive lethality of pmm-12 results from glycosylation defects rather than ascorbic acid depletion. Ref.6
Sequence similarities	Belongs to the eukaryotic PMM family.
Biophysicochemical properties	Kinetic parameters: Requires glucose-1,6-bisphosphate for activity. KM=29.7 µM for mannose-1-phosphate Ref.1 KM=65.4 µM for glucose-1-phosphate Vmax=14.4 µmol/min/mg enzyme with mannose-1-phosphate as substrate Vmax=1.4 µmol/min/mg enzyme with glucose-1-phosphate as substrate pH dependence: Optimum pH is 7.5. Temperature dependence: Optimum temperature is 30 degrees Celsius.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway L-ascorbic acid biosynthetic process Inferred from mutant phenotype Ref.1. Source: TAIR mannose biosynthetic process Inferred from electronic annotation. Source: InterPro response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	phosphomannomutase activity Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 246	246	Phosphomannomutase		PRO_0000199700
Sites
	Active site	13	1	Nucleophile By similarity
	Active site	15	1	By similarity
	Active site	48	1	By similarity
	Active site	190	1	By similarity
	Binding site	22	1	Substrate By similarity
	Binding site	124	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	142	1	Substrate By similarity
	Binding site	180	1	Substrate By similarity
	Binding site	182	1	Substrate By similarity
Experimental info
	Mutagenesis	7	1	G → R in pmm-1; 18% reduction of catalytic activity. In pmm-12/dgr1; 92% reduction of catalytic activity resulting in lethality when grown at restrictive temperature; when associated with Q-37. Ref.6
	Mutagenesis	37	1	R → Q in pmm-2; 86% reduction of catalytic activity. In pmm-12/dgr1; 92% reduction of catalytic activity resulting in lethality when grown at restrictive temperature; when associated with R-7. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O80840 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 52971A3F1AE08DF9	FASTA	246	27,762
	10 20 30 40 50 60 MAAKIPGVIA LFDVDGTLTA PRKEATPELL DFIRELRKVV TIGVVGGSDL SKISEQLGKT 70 80 90 100 110 120 VTNDYDYCFS ENGLVAHKDG KSIGIQSLKL HLGDDKLKEL INFTLHYIAD LDIPIKRGTF 130 140 150 160 170 180 IEFRNGMLNV SPIGRNCSQE ERDEFERYDK VQNIRPKMVA ELRERFAHLN LTFSIGGQIS 190 200 210 220 230 240 FDVFPKGWDK TYCLQYLEDF SEIHFFGDKT YEGGNDYEIY ESPKTIGHSV TSPDDTVAKC KALFMS

References

	« Hide 'large scale' referencesShow 'large scale' 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"A temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death." Hoeberichts F.A., Vaeck E., Kiddle G., Coppens E., van de Cotte B., Adamantidis A., Ormenese S., Foyer C.H., Zabeau M., Inze D., Perilleux C., Van Breusegem F., Vuylsteke M. J. Biol. Chem. 283:5708-5718(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-7 AND ARG-37, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ442991 mRNA. Translation: ABD97870.1. AC004665 Genomic DNA. Translation: AAC28545.1. CP002685 Genomic DNA. Translation: AEC10601.1. AY050806 mRNA. Translation: AAK92741.1. AY113964 mRNA. Translation: AAM45012.1. AY088930 mRNA. Translation: AAM67236.1.
IPI	IPI00517517.
PIR	T02468.
RefSeq	NP_182103.1. NM_130142.3.
UniGene	At.20569. At.48595.
3D structure databases
ProteinModelPortal	O80840.
SMR	O80840. Positions 6-244.
ModBase	Search...
Protein-protein interaction databases
IntAct	O80840. 1 interaction.
STRING	3702.AT2G45790.1-P.
Proteomic databases
PaxDb	O80840.
PRIDE	O80840.
Protocols and materials databases
DNASU	819187.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G45790.1; AT2G45790.1; AT2G45790.
GeneID	819187.
KEGG	ath:AT2G45790.
Organism-specific databases
TAIR	At2g45790.
Phylogenomic databases
eggNOG	COG0561.
HOGENOM	HOG000181843.
InParanoid	O80840.
KO	K01840.
OMA	EFERYDK.
PhylomeDB	O80840.
ProtClustDB	PLN02423.
Enzyme and pathway databases
BioCyc	MetaCyc:AT2G45790-MONOMER.
UniPathway	UPA00126; UER00424.
Gene expression databases
Genevestigator	O80840.
GermOnline	AT2G45790. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.50.1000. 2 hits.
InterPro	IPR023214. HAD-like_dom. IPR006379. HAD-SF_hydro_IIB. IPR005002. PMM. [Graphical view]
PANTHER	PTHR10466. PTHR10466. 1 hit.
Pfam	PF03332. PMM. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01484. HAD-SF-IIB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PMM_ARATH

Accession

Primary (citable) accession number: O80840
Secondary accession number(s): Q1W379

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program