ID   MPI1_ARATH              Reviewed;         432 AA.
AC   Q9M884;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Mannose-6-phosphate isomerase 1;
DE            EC=5.3.1.8 {ECO:0000269|PubMed:18755683};
DE   AltName: Full=Phosphohexomutase 1;
DE   AltName: Full=Phosphomannose isomerase 1;
DE            Short=PMI1;
DE   AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 31;
GN   Name=PMI1; Synonyms=MEE31; OrderedLocusNames=At3g02570;
GN   ORFNames=F16B3.20;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15634699; DOI=10.1242/dev.01595;
RA   Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA   Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT   "Genetic and molecular identification of genes required for female
RT   gametophyte development and function in Arabidopsis.";
RL   Development 132:603-614(2005).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, TISSUE SPECIFICITY, AND INDUCTION.
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).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Phosphomannose isomerase involved in the synthesis of the
CC       GDP-mannose and dolichol-phosphate-mannose required for a number of
CC       critical mannosyl transfer reactions. Involved in the ascorbic acid
CC       (AsA) biosynthesis. Required during the endosperm development.
CC       {ECO:0000269|PubMed:15634699, 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+), Co(2+), p-
CC       chloromercuribenzoate and L-ascorbic acid (AsA).
CC       {ECO:0000269|PubMed:18755683}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=41.3 uM for mannose-6-phosphate {ECO:0000269|PubMed:18755683};
CC         Vmax=1.89 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 52 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.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in both vegetative and
CC       reproductive organs under normal growth conditions (at protein level).
CC       {ECO:0000269|PubMed:18755683}.
CC   -!- INDUCTION: By light (at the protein level). Down-regulated by dark (at
CC       the protein level). Down-regulated by DCMU, an exogenous photosynthesis
CC       inhibitor. {ECO:0000269|PubMed:18755683}.
CC   -!- DISRUPTION PHENOTYPE: Endosperm development arrested.
CC       {ECO:0000269|PubMed:15634699}.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AC021640; AAF32464.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73831.1; -; Genomic_DNA.
DR   EMBL; AY070447; AAL49850.1; -; mRNA.
DR   EMBL; AY096564; AAM20214.1; -; mRNA.
DR   RefSeq; NP_186906.1; NM_111125.4.
DR   AlphaFoldDB; Q9M884; -.
DR   SMR; Q9M884; -.
DR   BioGRID; 5990; 1.
DR   IntAct; Q9M884; 1.
DR   STRING; 3702.Q9M884; -.
DR   iPTMnet; Q9M884; -.
DR   PaxDb; 3702-AT3G02570-1; -.
DR   ProteomicsDB; 250945; -.
DR   EnsemblPlants; AT3G02570.1; AT3G02570.1; AT3G02570.
DR   GeneID; 820656; -.
DR   Gramene; AT3G02570.1; AT3G02570.1; AT3G02570.
DR   KEGG; ath:AT3G02570; -.
DR   Araport; AT3G02570; -.
DR   TAIR; AT3G02570; MEE31.
DR   eggNOG; KOG2757; Eukaryota.
DR   HOGENOM; CLU_026967_0_0_1; -.
DR   InParanoid; Q9M884; -.
DR   OMA; DIGLFCG; -.
DR   OrthoDB; 1116301at2759; -.
DR   PhylomeDB; Q9M884; -.
DR   BioCyc; ARA:AT3G02570-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G02570-MONOMER; -.
DR   BRENDA; 5.3.1.8; 399.
DR   SABIO-RK; Q9M884; -.
DR   UniPathway; UPA00126; UER00423.
DR   PRO; PR:Q9M884; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M884; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:UniProtKB.
DR   GO; GO:0032025; P:response to cobalt ion; IEP:UniProtKB.
DR   GO; GO:0033591; P:response to L-ascorbic acid; IEP:UniProtKB.
DR   GO; GO:0009416; P:response to light stimulus; 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; 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:SF9; MANNOSE-6-PHOSPHATE ISOMERASE 1; 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   Genevisible; Q9M884; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Isomerase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..432
FT                   /note="Mannose-6-phosphate isomerase 1"
FT                   /id="PRO_0000420339"
FT   ACT_SITE        307
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   432 AA;  48566 MW;  9BF364B9BCF8FC9B CRC64;
     MEIATVVKAN GGCEADRRRL RRLRCSVKDY DWGKIGSDSL VYRVYAANSD YEIDPTRPYA
     ELWMGTHESG PSYLEDADGS NGVTLRSWIT ENPKSLGNRV LEKWGCDLPF LFKVLSVARP
     LSIQAHPDKK LAKKMHKAHP NLYKDDNHKP EMALAYTQFE ALCGFIPLQE LKSVIRAIPE
     IEELVGSEEA NQVFCITEHD EEKVKSVVRT IFTLLMSADA DTTKKIVSKL KRRLHMESQE
     RQLTDKERLV LKLEKQYPND IGVISAFFFN YVKLNPGEAL YLGANEPHAY LFGECLEVMA
     TSDNVVRAGL TSKPLDIQTL CSMLSYKLGY PEILKGTRIR PYITRYLPPF EEFEVDLCDL
     PSGASTVFPS VPGPSLLLVL QGEGRMSTEA SADGISMGDV LFVPADTEIH LRSSSDLKLY
     RAGINSRFLF PL
//