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Protein

Mannose-6-phosphate isomerase 2

Gene

PMI2

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.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

  • carbohydrate metabolic process Source: InterPro
  • 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
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Metal-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

TAIRiAT1G67070.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

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.
OMAiNYVKLEV.
OrthoDBiEOG09360AGB.
PhylomeDBiQ9FZH5.

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.
PS00966. PMI_I_2. 1 hit.
[Graphical view]

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.
AK176384 mRNA. Translation: BAD44147.1.
AK176481 mRNA. Translation: BAD44244.1.
BT025995 mRNA. Translation: ABG25084.1.
AF159377 mRNA. Translation: AAG23720.1.
PIRiE96694.
RefSeqiNP_176878.1. NM_105377.5.
UniGeneiAt.35695.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE96694.
RefSeqiNP_176878.1. NM_105377.5.
UniGeneiAt.35695.

3D structure databases

ProteinModelPortaliQ9FZH5.
SMRiQ9FZH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G67070.1.

Proteomic databases

PaxDbiQ9FZH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT1G67070.

Phylogenomic databases

eggNOGiKOG2757. Eukaryota.
COG1482. LUCA.
HOGENOMiHOG000241277.
KOiK01809.
OMAiNYVKLEV.
OrthoDBiEOG09360AGB.
PhylomeDBiQ9FZH5.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ9FZH5.

Gene expression databases

GenevisibleiQ9FZH5. AT.

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.
PS00966. PMI_I_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMPI2_ARATH
AccessioniPrimary (citable) accession number: Q9FZH5
Secondary accession number(s): Q67YT4, Q9FVM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 112 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

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 one 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.