INVE_ARATH
ID INVE_ARATH Reviewed; 617 AA.
AC Q9FK88;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Alkaline/neutral invertase E, chloroplastic {ECO:0000305};
DE Short=A/N-INVE {ECO:0000303|PubMed:21441406};
DE EC=3.2.1.26 {ECO:0000269|PubMed:20304912};
DE Flags: Precursor;
GN Name=INVE {ECO:0000303|PubMed:21441406};
GN OrderedLocusNames=At5g22510 {ECO:0000312|Araport:AT5G22510};
GN ORFNames=MQJ16.5 {ECO:0000312|EMBL:BAB09123.1};
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18034262; DOI=10.1007/s00425-007-0657-1;
RA Vargas W.A., Pontis H.G., Salerno G.L.;
RT "New insights on sucrose metabolism: evidence for an active A/N-Inv in
RT chloroplasts uncovers a novel component of the intracellular carbon
RT trafficking.";
RL Planta 227:795-807(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-294.
RX PubMed=20304912; DOI=10.1074/jbc.m109.055111;
RA Tamoi M., Tabuchi T., Demuratani M., Otori K., Tanabe N., Maruta T.,
RA Shigeoka S.;
RT "Point mutation of a plastidic invertase inhibits development of the
RT photosynthetic apparatus and enhances nitrate assimilation in sugar-treated
RT Arabidopsis seedlings.";
RL J. Biol. Chem. 285:15399-15407(2010).
RN [7]
RP GENE FAMILY.
RX PubMed=21441406; DOI=10.1093/jxb/err069;
RA Xiang L., Le Roy K., Bolouri-Moghaddam M.R., Vanhaecke M., Lammens W.,
RA Rolland F., Van den Ende W.;
RT "Exploring the neutral invertase-oxidative stress defence connection in
RT Arabidopsis thaliana.";
RL J. Exp. Bot. 62:3849-3862(2011).
CC -!- FUNCTION: Chloroplastic invertase that cleaves sucrose into glucose and
CC fructose and is associated with the development of the photosynthetic
CC apparatus and the assimilation of nitrogen in seedlings to control the
CC sucrose to hexose ratio (PubMed:20304912). Participates in the carbon
CC flux between the cytosol and plastids in leaves (PubMed:18034262).
CC {ECO:0000269|PubMed:18034262, ECO:0000269|PubMed:20304912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC Evidence={ECO:0000269|PubMed:20304912};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18034262}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:18034262}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the mutant plants accumulate decreased amount of starch
CC during the day. {ECO:0000269|PubMed:18034262}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 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; AB012244; BAB09123.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93035.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71174.1; -; Genomic_DNA.
DR EMBL; AY056449; AAL08305.1; -; mRNA.
DR EMBL; BT046120; ACI46508.1; -; mRNA.
DR RefSeq; NP_001332722.1; NM_001343739.1.
DR RefSeq; NP_197643.1; NM_122156.4.
DR AlphaFoldDB; Q9FK88; -.
DR SMR; Q9FK88; -.
DR STRING; 3702.AT5G22510.1; -.
DR CAZy; GH100; Glycoside Hydrolase Family 100.
DR PaxDb; Q9FK88; -.
DR PRIDE; Q9FK88; -.
DR ProMEX; Q9FK88; -.
DR ProteomicsDB; 247033; -.
DR EnsemblPlants; AT5G22510.1; AT5G22510.1; AT5G22510.
DR EnsemblPlants; AT5G22510.2; AT5G22510.2; AT5G22510.
DR GeneID; 832312; -.
DR Gramene; AT5G22510.1; AT5G22510.1; AT5G22510.
DR Gramene; AT5G22510.2; AT5G22510.2; AT5G22510.
DR KEGG; ath:AT5G22510; -.
DR Araport; AT5G22510; -.
DR TAIR; locus:2171112; AT5G22510.
DR eggNOG; ENOG502QPZ2; Eukaryota.
DR HOGENOM; CLU_020846_1_0_1; -.
DR InParanoid; Q9FK88; -.
DR OMA; NFHIREY; -.
DR OrthoDB; 389322at2759; -.
DR PhylomeDB; Q9FK88; -.
DR PRO; PR:Q9FK88; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK88; baseline and differential.
DR Genevisible; Q9FK88; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:TAIR.
DR GO; GO:0048825; P:cotyledon development; IMP:TAIR.
DR GO; GO:0005982; P:starch metabolic process; IMP:TAIR.
DR GO; GO:0005987; P:sucrose catabolic process; IDA:TAIR.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR024746; Glyco_hydro_100.
DR PANTHER; PTHR31916; PTHR31916; 1.
DR Pfam; PF12899; Glyco_hydro_100; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Glycosidase; Hydrolase;
KW Phosphoprotein; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..617
FT /note="Alkaline/neutral invertase E, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431501"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT MUTAGEN 294
FT /note="C->Y: In sicy-192; inhibition of cotyledon greening
FT when treated with sucrose; no effect on enzymatic
FT activity."
FT /evidence="ECO:0000269|PubMed:20304912"
SQ SEQUENCE 617 AA; 69240 MW; 04F09174C2F47325 CRC64;
MAASETVLRV PLGSVSQSCY LASFFVNSTP NLSFKPVSRN RKTVRCTNSH EVSSVPKHSF
HSSNSVLKGK KFVSTICKCQ KHDVEESIRS TLLPSDGLSS ELKSDLDEMP LPVNGSVSSN
GNAQSVGTKS IEDEAWDLLR QSVVFYCGSP IGTIAANDPN STSVLNYDQV FIRDFIPSGI
AFLLKGEYDI VRNFILYTLQ LQSWEKTMDC HSPGQGLMPC SFKVKTVPLD GDDSMTEEVL
DPDFGEAAIG RVAPVDSGLW WIILLRAYGK CTGDLSVQER VDVQTGIKMI LKLCLADGFD
MFPTLLVTDG SCMIDRRMGI HGHPLEIQAL FYSALVCARE MLTPEDGSAD LIRALNNRLV
ALNFHIREYY WLDLKKINEI YRYQTEEYSY DAVNKFNIYP DQIPSWLVDF MPNRGGYLIG
NLQPAHMDFR FFTLGNLWSI VSSLASNDQS HAILDFIEAK WAELVADMPL KICYPAMEGE
EWRIITGSDP KNTPWSYHNG GAWPTLLWQL TVASIKMGRP EIAEKAVELA ERRISLDKWP
EYYDTKRARF IGKQARLYQT WSIAGYLVAK LLLANPAAAK FLTSEEDSDL RNAFSCMLSA
NPRRTRGPKK AQQPFIV
