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Q9M884 (MPI1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 1
EC=5.3.1.8
Alternative name(s):
Phosphohexomutase 1
Phosphomannose isomerase 1
Short name=PMI1
Protein MATERNAL EFFECT EMBRYO ARREST 31
Gene names
Name:PMI1
Synonyms:MEE31
Ordered Locus Names:At3g02570
ORF Names:F16B3.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length432 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. Involved in the ascorbic acid (AsA) biosynthesis. Required during the endosperm development. Ref.4 Ref.5

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+, Co2+, p-chloromercuribenzoate and L-ascorbic acid (AsA). Ref.5

Pathway

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

Tissue specificity

Constitutively expressed in both vegetative and reproductive organs under normal growth conditions (at protein level). Ref.5

Induction

By light (at the protein level). Down-regulated by dark (at the protein level). Down-regulated by DCMU, an exogenous photosynthesis inhibitor. Ref.5

Disruption phenotype

Endosperm development arrested. Ref.4

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=41.3 µM for mannose-6-phosphate Ref.5

Vmax=1.89 µmol/min/mg enzyme with mannose-6-phosphate as substrate

pH dependence:

Optimum pH is 7.5.

Temperature dependence:

Optimum temperature is 52 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Mannose-6-phosphate isomerase 1
PRO_0000420339

Sites

Active site3071 By similarity
Metal binding1241Zinc By similarity
Metal binding1261Zinc By similarity
Metal binding1511Zinc By similarity
Metal binding2881Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9M884 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9BF364B9BCF8FC9B

FASTA43248,566
        10         20         30         40         50         60 
MEIATVVKAN GGCEADRRRL RRLRCSVKDY DWGKIGSDSL VYRVYAANSD YEIDPTRPYA 

        70         80         90        100        110        120 
ELWMGTHESG PSYLEDADGS NGVTLRSWIT ENPKSLGNRV LEKWGCDLPF LFKVLSVARP 

       130        140        150        160        170        180 
LSIQAHPDKK LAKKMHKAHP NLYKDDNHKP EMALAYTQFE ALCGFIPLQE LKSVIRAIPE 

       190        200        210        220        230        240 
IEELVGSEEA NQVFCITEHD EEKVKSVVRT IFTLLMSADA DTTKKIVSKL KRRLHMESQE 

       250        260        270        280        290        300 
RQLTDKERLV LKLEKQYPND IGVISAFFFN YVKLNPGEAL YLGANEPHAY LFGECLEVMA 

       310        320        330        340        350        360 
TSDNVVRAGL TSKPLDIQTL CSMLSYKLGY PEILKGTRIR PYITRYLPPF EEFEVDLCDL 

       370        380        390        400        410        420 
PSGASTVFPS VPGPSLLLVL QGEGRMSTEA SADGISMGDV LFVPADTEIH LRSSSDLKLY 

       430 
RAGINSRFLF PL

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(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]"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. expand/collapse author list , 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.
[4]"Genetic and molecular identification of genes required for female gametophyte development and function in Arabidopsis."
Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S., Capron A., Xie L.-F., Ye D., Sundaresan V.
Development 132:603-614(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC021640 Genomic DNA. Translation: AAF32464.1.
CP002686 Genomic DNA. Translation: AEE73831.1.
AY070447 mRNA. Translation: AAL49850.1.
AY096564 mRNA. Translation: AAM20214.1.
IPIIPI00521982.
RefSeqNP_186906.1. NM_111125.3.
UniGeneAt.18813.
At.24147.

3D structure databases

ProteinModelPortalQ9M884.
SMRQ9M884. Positions 19-426.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9M884. 1 interaction.
STRING3702.AT3G02570.1-P.

Proteomic databases

PaxDbQ9M884.
PRIDEQ9M884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G02570.1; AT3G02570.1; AT3G02570.
GeneID820656.
KEGGath:AT3G02570.

Organism-specific databases

TAIRAt3g02570.

Phylogenomic databases

eggNOGCOG1482.
HOGENOMHOG000241277.
InParanoidQ9M884.
KOK01809.
OMAACTPHAY.
PhylomeDBQ9M884.
ProtClustDBPLN02288.

Enzyme and pathway databases

BioCycMetaCyc:AT3G02570-MONOMER.
UniPathwayUPA00126; UER00423.

Gene expression databases

GenevestigatorQ9M884.

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. RmlC_like_cupin. 1 hit.
TIGRFAMsTIGR00218. manA. 1 hit.
PROSITEPS00965. PMI_I_1. 1 hit.
PS00966. PMI_I_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMPI1_ARATH
AccessionPrimary (citable) accession number: Q9M884
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: October 1, 2000
Last modified: May 29, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents