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 24-JAN-2024, entry version 147. 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; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q9FZH5; -. DR PaxDb; 3702-AT1G67070-1; -. 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; AT1G67070; DIN9. DR eggNOG; KOG2757; Eukaryota. DR HOGENOM; CLU_026967_2_1_1; -. DR InParanoid; Q9FZH5; -. DR OMA; VKILCSM; -. DR OrthoDB; 1116301at2759; -. DR PhylomeDB; Q9FZH5; -. DR BioCyc; ARA:AT1G67070-MONOMER; -. DR BioCyc; MetaCyc:AT1G67070-MONOMER; -. DR SABIO-RK; Q9FZH5; -. DR UniPathway; UPA00126; UER00423. DR PRO; PR:Q9FZH5; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9FZH5; baseline and differential. 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; IEA:UniProtKB-UniPathway. 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 CDD; cd07011; cupin_PMI_type_I_N; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 2. DR Gene3D; 1.10.441.10; Phosphomannose Isomerase, domain 2; 1. DR InterPro; IPR001250; Man6P_Isoase-1. DR InterPro; IPR016305; Mannose-6-P_Isomerase. DR InterPro; IPR018050; Pmannose_isomerase-type1_CS. DR InterPro; IPR046456; PMI_typeI_C. DR InterPro; IPR046457; PMI_typeI_cat. DR InterPro; IPR046458; PMI_typeI_hel. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR NCBIfam; TIGR00218; manA; 1. DR PANTHER; PTHR10309; MANNOSE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR10309:SF0; MANNOSE-6-PHOSPHATE ISOMERASE; 1. DR Pfam; PF01238; PMI_typeI_C; 1. DR Pfam; PF20511; PMI_typeI_cat; 1. DR Pfam; PF20512; PMI_typeI_hel; 1. DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1. DR PRINTS; PR00714; MAN6PISMRASE. DR SUPFAM; SSF51182; RmlC-like cupins; 1. DR PROSITE; PS00965; PMI_I_1; 1. DR PROSITE; PS00966; PMI_I_2; 1. DR Genevisible; Q9FZH5; AT. 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 //