MPI2_ARATH
ID MPI2_ARATH Reviewed; 441 AA.
AC Q9FZH5; Q67YT4; Q9FVM3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Mannose-6-phosphate isomerase 2;
DE EC=5.3.1.8 {ECO:0000269|PubMed:18755683};
DE AltName: Full=Phosphohexomutase 2;
DE AltName: Full=Phosphomannose isomerase 2;
DE Short=PMI2;
DE AltName: Full=Protein DARK INDUCIBLE 9;
GN Name=PMI2; Synonyms=DIN9; OrderedLocusNames=At1g67070; ORFNames=F1O19.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-240, INDUCTION BY DARK, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=11240919; DOI=10.1034/j.1399-3054.2001.1110312.x;
RA Fujiki Y., Yoshikawa Y., Sato T., Inada N., Ito M., Nishida I.,
RA Watanabe A.;
RT "Dark-inducible genes from Arabidopsis thaliana are associated with leaf
RT senescence and repressed by sugars.";
RL Physiol. Plantarum 111:345-352(2001).
RN [6]
RP INDUCTION.
RX PubMed=11080291; DOI=10.1104/pp.124.3.1139;
RA Fujiki Y., Ito M., Nishida I., Watanabe A.;
RT "Multiple signaling pathways in gene expression during sugar starvation.
RT Pharmacological analysis of din gene expression in suspension-cultured
RT cells of Arabidopsis.";
RL Plant Physiol. 124:1139-1148(2000).
RN [7]
RP INDUCTION BY DARK, AND DEVELOPMENTAL STAGE.
RX PubMed=16100230; DOI=10.1093/pcp/pci174;
RA Fujiki Y., Nakagawa Y., Furumoto T., Yoshida S., Biswal B., Ito M.,
RA Watanabe A., Nishida I.;
RT "Response to darkness of late-responsive dark-inducible genes is positively
RT regulated by leaf age and negatively regulated by calmodulin-antagonist-
RT sensitive signalling in Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:1741-1746(2005).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, INDUCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18755683; DOI=10.1074/jbc.m805538200;
RA Maruta T., Yonemitsu M., Yabuta Y., Tamoi M., Ishikawa T., Shigeoka S.;
RT "Arabidopsis phosphomannose isomerase 1, but not phosphomannose isomerase
RT 2, is essential for ascorbic acid biosynthesis.";
RL J. Biol. Chem. 283:28842-28851(2008).
CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-
CC phosphate-mannose required for a number of critical mannosyl transfer
CC reactions. {ECO:0000269|PubMed:18755683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC EC=5.3.1.8; Evidence={ECO:0000269|PubMed:18755683};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, Zn(2+), Cd(2+), DTT, p-
CC chloromercuribenzoate and L-ascorbic acid (AsA).
CC {ECO:0000269|PubMed:18755683}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=372 uM for mannose-6-phosphate {ECO:0000269|PubMed:18755683};
CC Vmax=22.5 umol/min/mg enzyme with mannose-6-phosphate as substrate
CC {ECO:0000269|PubMed:18755683};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18755683};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius.
CC {ECO:0000269|PubMed:18755683};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 1/2. {ECO:0000305|PubMed:18755683}.
CC -!- TISSUE SPECIFICITY: Not expressed in any organs under light (at protein
CC level). {ECO:0000269|PubMed:18755683}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the last stage of senescence in old
CC leaves. {ECO:0000269|PubMed:11240919, ECO:0000269|PubMed:16100230}.
CC -!- INDUCTION: By sugar starvation, by dark and by 3-O-methyl-Glc (3-OMG).
CC Down-regulated by sugars. Up-regulated by DCMU, an exogenous
CC photosynthesis inhibitor. {ECO:0000269|PubMed:11080291,
CC ECO:0000269|PubMed:11240919, ECO:0000269|PubMed:16100230,
CC ECO:0000269|PubMed:18755683}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AC007152; AAF98217.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34592.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59346.1; -; Genomic_DNA.
DR EMBL; AK176384; BAD44147.1; -; mRNA.
DR EMBL; AK176481; BAD44244.1; -; mRNA.
DR EMBL; BT025995; ABG25084.1; -; mRNA.
DR EMBL; AF159377; AAG23720.1; -; mRNA.
DR PIR; E96694; E96694.
DR RefSeq; NP_001319330.1; NM_001334269.1.
DR RefSeq; NP_176878.1; NM_105377.5.
DR AlphaFoldDB; Q9FZH5; -.
DR SMR; Q9FZH5; -.
DR STRING; 3702.AT1G67070.1; -.
DR PaxDb; Q9FZH5; -.
DR PRIDE; Q9FZH5; -.
DR ProteomicsDB; 238900; -.
DR EnsemblPlants; AT1G67070.1; AT1G67070.1; AT1G67070.
DR EnsemblPlants; AT1G67070.2; AT1G67070.2; AT1G67070.
DR GeneID; 843027; -.
DR Gramene; AT1G67070.1; AT1G67070.1; AT1G67070.
DR Gramene; AT1G67070.2; AT1G67070.2; AT1G67070.
DR KEGG; ath:AT1G67070; -.
DR Araport; AT1G67070; -.
DR TAIR; locus:2019748; AT1G67070.
DR eggNOG; KOG2757; Eukaryota.
DR HOGENOM; CLU_026967_2_1_1; -.
DR OMA; TEFRVLC; -.
DR OrthoDB; 1043197at2759; -.
DR PhylomeDB; Q9FZH5; -.
DR BioCyc; ARA:AT1G67070-MON; -.
DR BioCyc; MetaCyc:AT1G67070-MON; -.
DR SABIO-RK; Q9FZH5; -.
DR UniPathway; UPA00126; UER00423.
DR PRO; PR:Q9FZH5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZH5; baseline and differential.
DR Genevisible; Q9FZH5; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IEP:UniProtKB.
DR GO; GO:0046680; P:response to DDT; IEP:UniProtKB.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR GO; GO:0010043; P:response to zinc ion; IEP:UniProtKB.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR016305; Mannose-6-P_Isomerase.
DR InterPro; IPR018050; Pmannose_isomerase-type1_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR10309; PTHR10309; 1.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1.
DR PRINTS; PR00714; MAN6PISMRASE.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR00218; manA; 1.
DR PROSITE; PS00965; PMI_I_1; 1.
DR PROSITE; PS00966; PMI_I_2; 1.
PE 1: Evidence at protein level;
KW Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..441
FT /note="Mannose-6-phosphate isomerase 2"
FT /id="PRO_0000420340"
FT ACT_SITE 315
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 85
FT /note="S -> F (in Ref. 5; AAG23720)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="V -> A (in Ref. 5; AAG23720)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="R -> S (in Ref. 5; AAG23720)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="L -> W (in Ref. 3; BAD44147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49248 MW; 05D6F0820858D2B1 CRC64;
MGADAIQTNG HDQAKLTGGE EIQRLRCFVK NYEWGKLGPE SLVARLQEAN TGQRVDSEIP
YAEFWMGTHE SGPSHVEFGS GHGVSDKCMV TLKSWVLDNP NLLGSKVVDK WGCDLPFLFK
VLSVTKALSI QAHPNKALAE KLHREDPLLY RDNNHKPEIA LAVTPFQALC GFVTLKELKE
VITNVPEITE LVGSKAADQI FNVHEHDEDE RIKSVVRLIF TQLMSASNNE TKQVVSRMKN
RLLLETKHRE LSEKEKLVLE LEKQYTGDIG VISAFFFNYV KLNPGEALYL DANEPHAYIS
GDCVECMAAS DNVVRAGLTP KHRDVQTLCS MLTYKLGYPE ILKGFPLTPY VTRYLPPFDE
FEVDHCDLPR GKSTVFPAVP GPSVYLVIEG KGQLRTGSSK VLVNRGDVLF VPADIEIHVT
GESDVMKLYR AGVSSRFFQT L
