NIN1_ORYSJ
ID NIN1_ORYSJ Reviewed; 628 AA.
AC Q10MC0; A0A0N7KH58;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Neutral/alkaline invertase 1, mitochondrial {ECO:0000305};
DE Short=OsNIN1 {ECO:0000303|PubMed:17086397};
DE EC=3.2.1.26 {ECO:0000269|PubMed:17086397};
DE Flags: Precursor;
GN Name=NIN1 {ECO:0000303|PubMed:17086397};
GN OrderedLocusNames=Os03g0314800 {ECO:0000312|EMBL:BAF11850.1},
GN LOC_Os03g20020 {ECO:0000312|EMBL:ABF95611.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17086397; DOI=10.1007/s00425-006-0430-x;
RA Murayama S., Handa H.;
RT "Genes for alkaline/neutral invertase in rice: alkaline/neutral invertases
RT are located in plant mitochondria and also in plastids.";
RL Planta 225:1193-1203(2007).
CC -!- FUNCTION: Mitochondrial invertase that cleaves sucrose into glucose and
CC fructose. {ECO:0000269|PubMed:17086397}.
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:17086397};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:17086397};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17086397}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf and stems.
CC {ECO:0000269|PubMed:17086397}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
CC {ECO:0000305}.
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DR EMBL; AC145491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DP000009; ABF95611.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11850.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83897.1; -; Genomic_DNA.
DR EMBL; AK103334; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015632948.1; XM_015777462.1.
DR AlphaFoldDB; Q10MC0; -.
DR SMR; Q10MC0; -.
DR STRING; 4530.OS03T0314800-01; -.
DR PaxDb; Q10MC0; -.
DR PRIDE; Q10MC0; -.
DR EnsemblPlants; Os03t0314800-01; Os03t0314800-01; Os03g0314800.
DR GeneID; 4332650; -.
DR Gramene; Os03t0314800-01; Os03t0314800-01; Os03g0314800.
DR KEGG; osa:4332650; -.
DR eggNOG; ENOG502QT23; Eukaryota.
DR HOGENOM; CLU_020846_0_0_1; -.
DR InParanoid; Q10MC0; -.
DR OMA; PRDSWPE; -.
DR OrthoDB; 373994at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10MC0; OS.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0005987; P:sucrose catabolic process; IDA:UniProtKB.
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 Reference proteome; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..628
FT /note="Neutral/alkaline invertase 1, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431505"
FT REGION 79..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 397
FT /note="E -> V (in Ref. 5; AK103334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 70074 MW; 7863E15C75288BF6 CRC64;
MAAAAISHLR RGAPRHARAL LYLSTRRFSS SSAAGVAPLA AVAASARRLL STSVDSGASS
TGESYKPPLF DPFRAASLAS SAPPLESPPI EELPDDATPP PEEEPGLPAP EKDPVATACQ
HELEGLKAWV ETVRSRKEST EEKEAWSLLG RSVVSYCGTA VGTVAANDPS TANQMLNYDQ
VFIRDFVPSA IAFLLKGEGD IVKNFLLHTL QLQSWEKTVD CYSPGQGLMP ASFKVRSIPL
DGNSEAFEEV LDPDFGESAI GRVAPVDSGL WWIILLRAYG KITGDYALQE RVDVQTGIRL
ILNLCLSDGF DMFPTLLVTD GSCMIDRRMG IHGHPLEIQS LFYSALRCAR EMVSVNDGSN
SLIRAINYRL SALSFHIREY YWVDMKKINE IYRYKTEEYS HDAINKFNIY PEQIPSWLAD
WIPEKGGYLI GNLQPAHMDF RFFSLGNLWA IISSLATQRQ AEGILNLIEA KWEDIIANMP
LKICYPALEY EEWRIITGSD PKNTPWSYHN GGSWPTLLWQ FTLACIKMGR RDLAQRAIEV
AEKRLSEDKW PEYYDTRTGR FIGKQSRLYQ TWTIAGYLSS KMLLDCPELA SILICEEDLE
LLEGCACSVN KSARTKCSRR AARSQVLV
