Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mannose-6-phosphate isomerase 2

Gene

PMI2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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.1 Publication

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+, DTT, p-chloromercuribenzoate and L-ascorbic acid (AsA).1 Publication

Kineticsi

  1. KM=372 µM for mannose-6-phosphate1 Publication
  1. Vmax=22.5 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 48 degrees Celsius.1 Publication

Pathwayi: 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), Phosphomannomutase (AXX17_At2g43390)
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)DescriptionActionsGraphical viewLength
Metal bindingi131ZincBy similarity1
Metal bindingi133ZincBy similarity1
Metal bindingi158ZincBy similarity1
Metal bindingi296ZincBy similarity1
Active sitei315By similarity1

GO - Molecular functioni

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

GO - Biological processi

  • cell wall mannoprotein biosynthetic process Source: GO_Central
  • GDP-mannose biosynthetic process Source: GO_Central
  • L-ascorbic acid biosynthetic process Source: TAIR
  • protein glycosylation Source: GO_Central
  • response to absence of light Source: UniProtKB
  • response to cadmium ion Source: UniProtKB
  • response to DDT Source: UniProtKB
  • response to L-ascorbic acid Source: UniProtKB
  • response to sucrose Source: UniProtKB
  • response to zinc ion Source: UniProtKB

Keywordsi

Molecular functionIsomerase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT1G67070-MONOMER
MetaCyc:AT1G67070-MONOMER
ReactomeiR-ATH-446205 Synthesis of GDP-mannose
SABIO-RKQ9FZH5
UniPathwayiUPA00126; UER00423

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PMI2
Synonyms:DIN9
Ordered Locus Names:At1g67070
ORF Names:F1O19.12
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

AraportiAT1G67070
TAIRilocus:2019748 AT1G67070

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004203401 – 441Mannose-6-phosphate isomerase 2Add BLAST441

Proteomic databases

PaxDbiQ9FZH5

Expressioni

Tissue specificityi

Not expressed in any organs under light (at protein level).1 Publication

Developmental stagei

Expressed at the last stage of senescence in old leaves.2 Publications

Inductioni

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.4 Publications

Gene expression databases

ExpressionAtlasiQ9FZH5 baseline and differential
GenevisibleiQ9FZH5 AT

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G67070.1

Structurei

3D structure databases

ProteinModelPortaliQ9FZH5
SMRiQ9FZH5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2757 Eukaryota
COG1482 LUCA
HOGENOMiHOG000241277
KOiK01809
OMAiLCYEKLM
OrthoDBiEOG09360AGB
PhylomeDBiQ9FZH5

Family and domain databases

Gene3Di2.60.120.10, 4 hits
InterProiView protein in InterPro
IPR001250 Man6P_Isoase-1
IPR016305 Mannose-6-P_Isomerase
IPR018050 Pmannose_isomerase-type1_CS
IPR014710 RmlC-like_jellyroll
IPR011051 RmlC_Cupin_sf
PANTHERiPTHR10309 PTHR10309, 1 hit
PfamiView protein in Pfam
PF01238 PMI_typeI, 1 hit
PIRSFiPIRSF001480 Mannose-6-phosphate_isomerase, 1 hit
PRINTSiPR00714 MAN6PISMRASE
SUPFAMiSSF51182 SSF51182, 1 hit
TIGRFAMsiTIGR00218 manA, 1 hit
PROSITEiView protein in PROSITE
PS00965 PMI_I_1, 1 hit
PS00966 PMI_I_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9FZH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGADAIQTNG HDQAKLTGGE EIQRLRCFVK NYEWGKLGPE SLVARLQEAN
60 70 80 90 100
TGQRVDSEIP YAEFWMGTHE SGPSHVEFGS GHGVSDKCMV TLKSWVLDNP
110 120 130 140 150
NLLGSKVVDK WGCDLPFLFK VLSVTKALSI QAHPNKALAE KLHREDPLLY
160 170 180 190 200
RDNNHKPEIA LAVTPFQALC GFVTLKELKE VITNVPEITE LVGSKAADQI
210 220 230 240 250
FNVHEHDEDE RIKSVVRLIF TQLMSASNNE TKQVVSRMKN RLLLETKHRE
260 270 280 290 300
LSEKEKLVLE LEKQYTGDIG VISAFFFNYV KLNPGEALYL DANEPHAYIS
310 320 330 340 350
GDCVECMAAS DNVVRAGLTP KHRDVQTLCS MLTYKLGYPE ILKGFPLTPY
360 370 380 390 400
VTRYLPPFDE FEVDHCDLPR GKSTVFPAVP GPSVYLVIEG KGQLRTGSSK
410 420 430 440
VLVNRGDVLF VPADIEIHVT GESDVMKLYR AGVSSRFFQT L
Length:441
Mass (Da):49,248
Last modified:March 1, 2001 - v1
Checksum:i05D6F0820858D2B1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti85S → F in AAG23720 (PubMed:11240919).Curated1
Sequence conflicti90V → A in AAG23720 (PubMed:11240919).Curated1
Sequence conflicti211R → S in AAG23720 (PubMed:11240919).Curated1
Sequence conflicti288L → W in BAD44147 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007152 Genomic DNA Translation: AAF98217.1
CP002684 Genomic DNA Translation: AEE34592.1
CP002684 Genomic DNA Translation: ANM59346.1
AK176384 mRNA Translation: BAD44147.1
AK176481 mRNA Translation: BAD44244.1
BT025995 mRNA Translation: ABG25084.1
AF159377 mRNA Translation: AAG23720.1
PIRiE96694
RefSeqiNP_001319330.1, NM_001334269.1
NP_176878.1, NM_105377.5
UniGeneiAt.35695

Genome annotation databases

EnsemblPlantsiAT1G67070.1; AT1G67070.1; AT1G67070
AT1G67070.2; AT1G67070.2; AT1G67070
GeneIDi843027
GrameneiAT1G67070.1; AT1G67070.1; AT1G67070
AT1G67070.2; AT1G67070.2; AT1G67070
KEGGiath:AT1G67070

Similar proteinsi

Entry informationi

Entry nameiMPI2_ARATH
AccessioniPrimary (citable) accession number: Q9FZH5
Secondary accession number(s): Q67YT4, Q9FVM3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: March 1, 2001
Last modified: April 25, 2018
This is version 120 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health