INVA_ARATH
ID INVA_ARATH Reviewed; 616 AA.
AC Q9FXA8;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Alkaline/neutral invertase A, mitochondrial {ECO:0000305};
DE Short=A/N-INVA {ECO:0000303|PubMed:21441406};
DE EC=3.2.1.26 {ECO:0000269|PubMed:21441406};
DE Flags: Precursor;
GN Name=INVA {ECO:0000303|PubMed:21441406};
GN OrderedLocusNames=At1g56560 {ECO:0000312|Araport:AT1G56560};
GN ORFNames=F25P12.99 {ECO:0000312|EMBL:AAG09107.1};
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=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;
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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION BY HYDROGEN
RP PEROXIDE, GENE FAMILY, AND DISRUPTION PHENOTYPE.
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).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23135328; DOI=10.1007/s00425-012-1794-8;
RA Martin M.L., Lechner L., Zabaleta E.J., Salerno G.L.;
RT "A mitochondrial alkaline/neutral invertase isoform (A/N-InvC) functions in
RT developmental energy-demanding processes in Arabidopsis.";
RL Planta 237:813-822(2013).
CC -!- FUNCTION: Mitochondrial invertase that cleaves sucrose into glucose and
CC fructose and is involved in the regulation of multiple tissue
CC development and floral transition. May generate glucose as a substrate
CC for mitochondria-associated hexokinase, contributing to mitochondrial
CC reactive oxygen species homeostasis. {ECO:0000269|PubMed:21441406}.
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:21441406};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 mM for sucrose {ECO:0000269|PubMed:21441406};
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:21441406};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21441406}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots and flowers.
CC {ECO:0000269|PubMed:23135328}.
CC -!- INDUCTION: By hydrogen peroxide (H(2)O(2)).
CC {ECO:0000269|PubMed:21441406}.
CC -!- DISRUPTION PHENOTYPE: Reduced primary root length and number of lateral
CC roots. Reduced plant growth, delayed flowering, increased expression of
CC antioxidant genes under basal conditions and reduced oxygen consumption
CC in the dark. {ECO:0000269|PubMed:21441406,
CC ECO:0000269|PubMed:23135328}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
CC {ECO:0000305}.
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DR EMBL; AC009323; AAG09107.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33409.1; -; Genomic_DNA.
DR EMBL; AY120777; AAM53335.1; -; mRNA.
DR EMBL; BT008387; AAP37746.1; -; mRNA.
DR PIR; C96607; C96607.
DR RefSeq; NP_176049.1; NM_104533.4.
DR AlphaFoldDB; Q9FXA8; -.
DR SMR; Q9FXA8; -.
DR STRING; 3702.AT1G56560.1; -.
DR CAZy; GH100; Glycoside Hydrolase Family 100.
DR PaxDb; Q9FXA8; -.
DR PRIDE; Q9FXA8; -.
DR ProteomicsDB; 247031; -.
DR EnsemblPlants; AT1G56560.1; AT1G56560.1; AT1G56560.
DR GeneID; 842110; -.
DR Gramene; AT1G56560.1; AT1G56560.1; AT1G56560.
DR KEGG; ath:AT1G56560; -.
DR Araport; AT1G56560; -.
DR TAIR; locus:2027600; AT1G56560.
DR eggNOG; ENOG502QT23; Eukaryota.
DR HOGENOM; CLU_020846_0_0_1; -.
DR InParanoid; Q9FXA8; -.
DR OMA; SFERIHV; -.
DR OrthoDB; 373994at2759; -.
DR PhylomeDB; Q9FXA8; -.
DR PRO; PR:Q9FXA8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXA8; baseline and differential.
DR Genevisible; Q9FXA8; AT.
DR GO; GO:0005739; C:mitochondrion; 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:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0005987; P:sucrose catabolic process; IMP: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; Glycosidase; Hydrolase; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..78
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 79..616
FT /note="Alkaline/neutral invertase A, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431497"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQF2"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LQF2"
SQ SEQUENCE 616 AA; 70437 MW; CA365D49D91B3C7E CRC64;
MSAIYLLRKI STKTPSRFHR SLFFSTFSKD SPPDLSRTTS IRHLSSSQRF VSSSIYCFPQ
SKILPNRFSE KTTGISVRQF STSVETNLSD KSFERIHVQS DAILERIHKN EEEVETVSIG
SEKVVREESE AEKEAWRILE NAVVRYCGSP VGTVAANDPG DKMPLNYDQV FIRDFVPSAL
AFLLKGEGDI VRNFLLHTLQ LQSWEKTVDC YSPGQGLMPA SFKVRTVALD ENTTEEVLDP
DFGESAIGRV APVDSGLWWI ILLRAYGKIT GDFSLQERID VQTGIKLIMN LCLADGFDMF
PTLLVTDGSC MIDRRMGIHG HPLEIQSLFY SALRCSREML SVNDSSKDLV RAINNRLSAL
SFHIREYYWV DIKKINEIYR YKTEEYSTDA TNKFNIYPEQ IPPWLMDWIP EQGGYLLGNL
QPAHMDFRFF TLGNFWSIVS SLATPKQNEA ILNLIEAKWD DIIGNMPLKI CYPALEYDDW
RIITGSDPKN TPWSYHNSGS WPTLLWQFTL ACMKMGRPEL AEKALAVAEK RLLADRWPEY
YDTRSGKFIG KQSRLYQTWT VAGFLTSKLL LANPEMASLL FWEEDYELLD ICACGLRKSD
RKKCSRVAAK TQILVR
