Q1W374 (PMM_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phosphomannomutase EC=5.4.2.8 Alternative name(s): TaPMM
Organism	Triticum aestivum (Wheat)
Taxonomic identifier	4565 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
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-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.
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 – 249	249	Phosphomannomutase		PRO_0000326497
Sites
	Active site	15	1	Nucleophile By similarity
	Active site	17	1	By similarity
	Active site	50	1	By similarity
	Active site	192	1	By similarity
	Binding site	24	1	Substrate By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	144	1	Substrate By similarity
	Binding site	182	1	Substrate By similarity
	Binding site	184	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1W374 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: AB85F0AB97DCD566	FASTA	249	28,252
	10 20 30 40 50 60 MAAARKDAGV LALFDVDGTL TAPRKEVTPE MLEFMKRLRE NVTVGVVGGS DLVKISEQLG 70 80 90 100 110 120 KSVITDYDYV FSENGLVAHK DGKLIGTQSL KTYLGDDQLK EFINFTLHYI ADLDIPIKRG 130 140 150 160 170 180 TFIEFRSGMI NVSPIGRNCS QEERDDFEKY DKVHNVRPKM VSVLREKFAH LNLTFSIGGQ 190 200 210 220 230 240 ISFDVFPQGW DKTYCLRYLE EFKEIHFFGD KTYKGGNDHE IFESDRTVGH TVTSPNDTVQ QCKSIFLSE

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
EMBL GenBank DDBJ	DQ442996 mRNA. Translation: ABD97875.1.
UniGene	Ta.3539.
3D structure databases
ProteinModelPortal	Q1W374.
SMR	Q1W374. Positions 11-246.
ModBase	Search...
Proteomic databases
PRIDE	Q1W374.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR023214. HAD-like_dom. IPR006379. HAD-SF_hydro_IIB. IPR005002. PMM. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
PANTHER	PTHR10466. PMM. 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_WHEAT

Accession

Primary (citable) accession number: Q1W374

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 2, 2006
Last modified:	June 28, 2011
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program