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Q9FZH5 (MPI2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannose-6-phosphate isomerase 2

EC=5.3.1.8
Alternative name(s):
Phosphohexomutase 2
Phosphomannose isomerase 2
Short name=PMI2
Protein DARK INDUCIBLE 9
Gene names
Name:PMI2
Synonyms:DIN9
Ordered Locus Names:At1g67070
ORF Names:F1O19.12
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. Ref.8

Catalytic activity

D-mannose 6-phosphate = D-fructose 6-phosphate.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by EDTA, Zn2+, Cd2+, DTT, p-chloromercuribenzoate and L-ascorbic acid (AsA). Ref.8

Pathway

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.

Tissue specificity

Not expressed in any organs under light (at protein level). Ref.8

Developmental stage

Expressed at the last stage of senescence in old leaves. Ref.5 Ref.7

Induction

By sugar starvation, by dark and by 3-O-methyl-Glc (3-OMG). Down-regulated by sugars. Up-regulated by DCMU, an exogenous photosynthesis inhibitor. Ref.5 Ref.6 Ref.7 Ref.8

Sequence similarities

Belongs to the mannose-6-phosphate isomerase type 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=372 µM for mannose-6-phosphate Ref.8

Vmax=22.5 µmol/min/mg enzyme with mannose-6-phosphate as substrate

pH dependence:

Optimum pH is 7.5.

Temperature dependence:

Optimum temperature is 48 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Mannose-6-phosphate isomerase 2
PRO_0000420340

Sites

Active site3151 By similarity
Metal binding1311Zinc By similarity
Metal binding1331Zinc By similarity
Metal binding1581Zinc By similarity
Metal binding2961Zinc By similarity

Experimental info

Sequence conflict851S → F in AAG23720. Ref.5
Sequence conflict901V → A in AAG23720. Ref.5
Sequence conflict2111R → S in AAG23720. Ref.5
Sequence conflict2881L → W in BAD44147. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9FZH5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 05D6F0820858D2B1

FASTA44149,248
        10         20         30         40         50         60 
MGADAIQTNG HDQAKLTGGE EIQRLRCFVK NYEWGKLGPE SLVARLQEAN TGQRVDSEIP 

        70         80         90        100        110        120 
YAEFWMGTHE SGPSHVEFGS GHGVSDKCMV TLKSWVLDNP NLLGSKVVDK WGCDLPFLFK 

       130        140        150        160        170        180 
VLSVTKALSI QAHPNKALAE KLHREDPLLY RDNNHKPEIA LAVTPFQALC GFVTLKELKE 

       190        200        210        220        230        240 
VITNVPEITE LVGSKAADQI FNVHEHDEDE RIKSVVRLIF TQLMSASNNE TKQVVSRMKN 

       250        260        270        280        290        300 
RLLLETKHRE LSEKEKLVLE LEKQYTGDIG VISAFFFNYV KLNPGEALYL DANEPHAYIS 

       310        320        330        340        350        360 
GDCVECMAAS DNVVRAGLTP KHRDVQTLCS MLTYKLGYPE ILKGFPLTPY VTRYLPPFDE 

       370        380        390        400        410        420 
FEVDHCDLPR GKSTVFPAVP GPSVYLVIEG KGQLRTGSSK VLVNRGDVLF VPADIEIHVT 

       430        440 
GESDVMKLYR AGVSSRFFQT L 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Arabidopsis ORF clones."
Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Dark-inducible genes from Arabidopsis thaliana are associated with leaf senescence and repressed by sugars."
Fujiki Y., Yoshikawa Y., Sato T., Inada N., Ito M., Nishida I., Watanabe A.
Physiol. Plantarum 111:345-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-240, INDUCTION BY DARK, DEVELOPMENTAL STAGE.
Strain: cv. Columbia.
[6]"Multiple signaling pathways in gene expression during sugar starvation. Pharmacological analysis of din gene expression in suspension-cultured cells of Arabidopsis."
Fujiki Y., Ito M., Nishida I., Watanabe A.
Plant Physiol. 124:1139-1148(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Response to darkness of late-responsive dark-inducible genes is positively regulated by leaf age and negatively regulated by calmodulin-antagonist-sensitive signalling in Arabidopsis thaliana."
Fujiki Y., Nakagawa Y., Furumoto T., Yoshida S., Biswal B., Ito M., Watanabe A., Nishida I.
Plant Cell Physiol. 46:1741-1746(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY DARK, DEVELOPMENTAL STAGE.
[8]"Arabidopsis phosphomannose isomerase 1, but not phosphomannose isomerase 2, is essential for ascorbic acid biosynthesis."
Maruta T., Yonemitsu M., Yabuta Y., Tamoi M., Ishikawa T., Shigeoka S.
J. Biol. Chem. 283:28842-28851(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC007152 Genomic DNA. Translation: AAF98217.1.
CP002684 Genomic DNA. Translation: AEE34592.1.
AK176384 mRNA. Translation: BAD44147.1.
AK176481 mRNA. Translation: BAD44244.1.
BT025995 mRNA. Translation: ABG25084.1.
AF159377 mRNA. Translation: AAG23720.1.
PIRE96694.
RefSeqNP_176878.1. NM_105377.4.
UniGeneAt.35695.

3D structure databases

ProteinModelPortalQ9FZH5.
SMRQ9FZH5. Positions 20-423.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9FZH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G67070.1; AT1G67070.1; AT1G67070.
GeneID843027.
KEGGath:AT1G67070.

Organism-specific databases

TAIRAT1G67070.

Phylogenomic databases

HOGENOMHOG000241277.
InParanoidQ9FZH5.
KOK01809.
OMAQEANTGQ.
PhylomeDBQ9FZH5.
ProtClustDBPLN02288.

Enzyme and pathway databases

BioCycARA:AT1G67070-MONOMER.
MetaCyc:AT1G67070-MONOMER.
UniPathwayUPA00126; UER00423.

Gene expression databases

ArrayExpressQ9FZH5.
GenevestigatorQ9FZH5.

Family and domain databases

Gene3D2.60.120.10. 3 hits.
InterProIPR001250. Man6P_Isoase-1.
IPR016305. Mannose-6-P_Isomerase.
IPR018050. Pmannose_isomerase-type1_CS.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR10309. PTHR10309. 1 hit.
PfamPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFPIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTSPR00714. MAN6PISMRASE.
SUPFAMSSF51182. SSF51182. 1 hit.
TIGRFAMsTIGR00218. manA. 1 hit.
PROSITEPS00965. PMI_I_1. 1 hit.
PS00966. PMI_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9FZH5.

Entry information

Entry nameMPI2_ARATH
AccessionPrimary (citable) accession number: Q9FZH5
Secondary accession number(s): Q67YT4, Q9FVM3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names