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Protein

Mannose-6-phosphate isomerase 1

Gene

PMI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by EDTA, Zn2+, Cd2+, Co2+, p-chloromercuribenzoate and L-ascorbic acid (AsA).1 Publication

Kineticsi

  1. KM=41.3 µM for mannose-6-phosphate1 Publication
  1. Vmax=1.89 µmol/min/mg enzyme with mannose-6-phosphate as substrate1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 52 degrees Celsius.1 Publication

Pathway: GDP-alpha-D-mannose biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Mannose-6-phosphate isomerase 1 (PMI1), Mannose-6-phosphate isomerase 2 (PMI2)
  2. Phosphomannomutase (PMM)
This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi124 – 1241ZincBy similarity
Metal bindingi126 – 1261ZincBy similarity
Metal bindingi151 – 1511ZincBy similarity
Metal bindingi288 – 2881ZincBy similarity
Active sitei307 – 3071By similarity

GO - Molecular functioni

  • mannose-6-phosphate isomerase activity Source: TAIR
  • zinc ion binding Source: InterPro

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • embryo development ending in seed dormancy Source: TAIR
  • GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  • response to cadmium ion Source: UniProtKB
  • response to cobalt ion Source: UniProtKB
  • response to L-ascorbic acid Source: UniProtKB
  • response to light stimulus Source: UniProtKB
  • response to zinc ion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT3G02570-MONOMER.
MetaCyc:AT3G02570-MONOMER.
BRENDAi5.3.1.8. 399.
ReactomeiREACT_325410. Synthesis of GDP-mannose.
SABIO-RKQ9M884.
UniPathwayiUPA00126; UER00423.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PMI1
Synonyms:MEE31
Ordered Locus Names:At3g02570
ORF Names:F16B3.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G02570.

Pathology & Biotechi

Disruption phenotypei

Endosperm development arrested.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Mannose-6-phosphate isomerase 1PRO_0000420339Add
BLAST

Proteomic databases

PaxDbiQ9M884.
PRIDEiQ9M884.

Expressioni

Tissue specificityi

Constitutively expressed in both vegetative and reproductive organs under normal growth conditions (at protein level).1 Publication

Inductioni

By light (at the protein level). Down-regulated by dark (at the protein level). Down-regulated by DCMU, an exogenous photosynthesis inhibitor.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi5990. 1 interaction.
IntActiQ9M884. 1 interaction.
STRINGi3702.AT3G02570.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M884.
SMRiQ9M884. Positions 19-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1482.
HOGENOMiHOG000241277.
InParanoidiQ9M884.
KOiK01809.
OMAiDSEPHAY.
PhylomeDBiQ9M884.

Family and domain databases

Gene3Di2.60.120.10. 3 hits.
InterProiIPR001250. Man6P_Isoase-1.
IPR016305. Mannose-6-P_Isomerase.
IPR018050. Pmannose_isomerase-type1_CS.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR10309. PTHR10309. 1 hit.
PfamiPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFiPIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTSiPR00714. MAN6PISMRASE.
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR00218. manA. 1 hit.
PROSITEiPS00965. PMI_I_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9M884-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIATVVKAN GGCEADRRRL RRLRCSVKDY DWGKIGSDSL VYRVYAANSD
60 70 80 90 100
YEIDPTRPYA ELWMGTHESG PSYLEDADGS NGVTLRSWIT ENPKSLGNRV
110 120 130 140 150
LEKWGCDLPF LFKVLSVARP LSIQAHPDKK LAKKMHKAHP NLYKDDNHKP
160 170 180 190 200
EMALAYTQFE ALCGFIPLQE LKSVIRAIPE IEELVGSEEA NQVFCITEHD
210 220 230 240 250
EEKVKSVVRT IFTLLMSADA DTTKKIVSKL KRRLHMESQE RQLTDKERLV
260 270 280 290 300
LKLEKQYPND IGVISAFFFN YVKLNPGEAL YLGANEPHAY LFGECLEVMA
310 320 330 340 350
TSDNVVRAGL TSKPLDIQTL CSMLSYKLGY PEILKGTRIR PYITRYLPPF
360 370 380 390 400
EEFEVDLCDL PSGASTVFPS VPGPSLLLVL QGEGRMSTEA SADGISMGDV
410 420 430
LFVPADTEIH LRSSSDLKLY RAGINSRFLF PL
Length:432
Mass (Da):48,566
Last modified:October 1, 2000 - v1
Checksum:i9BF364B9BCF8FC9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC021640 Genomic DNA. Translation: AAF32464.1.
CP002686 Genomic DNA. Translation: AEE73831.1.
AY070447 mRNA. Translation: AAL49850.1.
AY096564 mRNA. Translation: AAM20214.1.
RefSeqiNP_186906.1. NM_111125.3.
UniGeneiAt.18813.
At.24147.

Genome annotation databases

EnsemblPlantsiAT3G02570.1; AT3G02570.1; AT3G02570.
GeneIDi820656.
KEGGiath:AT3G02570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC021640 Genomic DNA. Translation: AAF32464.1.
CP002686 Genomic DNA. Translation: AEE73831.1.
AY070447 mRNA. Translation: AAL49850.1.
AY096564 mRNA. Translation: AAM20214.1.
RefSeqiNP_186906.1. NM_111125.3.
UniGeneiAt.18813.
At.24147.

3D structure databases

ProteinModelPortaliQ9M884.
SMRiQ9M884. Positions 19-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5990. 1 interaction.
IntActiQ9M884. 1 interaction.
STRINGi3702.AT3G02570.1.

Proteomic databases

PaxDbiQ9M884.
PRIDEiQ9M884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G02570.1; AT3G02570.1; AT3G02570.
GeneIDi820656.
KEGGiath:AT3G02570.

Organism-specific databases

TAIRiAT3G02570.

Phylogenomic databases

eggNOGiCOG1482.
HOGENOMiHOG000241277.
InParanoidiQ9M884.
KOiK01809.
OMAiDSEPHAY.
PhylomeDBiQ9M884.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00423.
BioCyciARA:AT3G02570-MONOMER.
MetaCyc:AT3G02570-MONOMER.
BRENDAi5.3.1.8. 399.
ReactomeiREACT_325410. Synthesis of GDP-mannose.
SABIO-RKQ9M884.

Miscellaneous databases

PROiQ9M884.

Family and domain databases

Gene3Di2.60.120.10. 3 hits.
InterProiIPR001250. Man6P_Isoase-1.
IPR016305. Mannose-6-P_Isomerase.
IPR018050. Pmannose_isomerase-type1_CS.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR10309. PTHR10309. 1 hit.
PfamiPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFiPIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTSiPR00714. MAN6PISMRASE.
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR00218. manA. 1 hit.
PROSITEiPS00965. PMI_I_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMPI1_ARATH
AccessioniPrimary (citable) accession number: Q9M884
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.