MPI1_ARATH
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 03-AUG-2022, entry version 141.
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; 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.AT3G02570.1; -.
DR iPTMnet; Q9M884; -.
DR PaxDb; Q9M884; -.
DR PRIDE; Q9M884; -.
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; locus:2076864; AT3G02570.
DR eggNOG; KOG2757; Eukaryota.
DR HOGENOM; CLU_026967_0_0_1; -.
DR InParanoid; Q9M884; -.
DR OMA; DIGLFCG; -.
DR OrthoDB; 1043197at2759; -.
DR PhylomeDB; Q9M884; -.
DR BioCyc; ARA:AT3G02570-MON; -.
DR BioCyc; MetaCyc:AT3G02570-MON; -.
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 Genevisible; Q9M884; 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: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; IBA:GO_Central.
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 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.
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
