SPP3B_ARATH
ID SPP3B_ARATH Reviewed; 423 AA.
AC Q93XN8; Q8RWS3; Q9FT48;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Probable sucrose-phosphatase 3b;
DE Short=AtSPP3b;
DE EC=3.1.3.24;
GN Name=SPP3B; Synonyms=SPP2; OrderedLocusNames=At3g52340;
GN ORFNames=T25B15.110;
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 [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Seed;
RX PubMed=11050182; DOI=10.1073/pnas.230430197;
RA Lunn J.E., Ashton A.R., Hatch M.D., Heldt H.W.;
RT "Purification, molecular cloning, and sequence analysis of sucrose-6F-
RT phosphate phosphohydrolase from plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12914-12919(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12559580; DOI=10.1016/s0378-1119(02)01177-0;
RA Lunn J.E.;
RT "Sucrose-phosphatase gene families in plants.";
RL Gene 303:187-196(2003).
CC -!- FUNCTION: Catalyzes the final step of sucrose synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sucrose 6(F)-phosphate = phosphate + sucrose;
CC Xref=Rhea:RHEA:19289, ChEBI:CHEBI:15377, ChEBI:CHEBI:17992,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57723; EC=3.1.3.24;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93XN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93XN8-2; Sequence=VSP_035433, VSP_035434;
CC -!- SIMILARITY: Belongs to the sucrose phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC07925.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF356816; AAK40235.1; -; mRNA.
DR EMBL; AL132972; CAC07925.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78934.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78935.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78936.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64820.1; -; Genomic_DNA.
DR EMBL; AY091146; AAM14095.1; -; mRNA.
DR EMBL; BT000909; AAN41309.1; -; mRNA.
DR EMBL; AK175395; BAD43158.1; -; mRNA.
DR PIR; T46104; T46104.
DR RefSeq; NP_001030846.1; NM_001035769.3. [Q93XN8-1]
DR RefSeq; NP_001326825.1; NM_001339572.1. [Q93XN8-1]
DR RefSeq; NP_566964.1; NM_115094.4. [Q93XN8-1]
DR RefSeq; NP_974417.1; NM_202688.2. [Q93XN8-1]
DR AlphaFoldDB; Q93XN8; -.
DR SMR; Q93XN8; -.
DR BioGRID; 9717; 1.
DR IntAct; Q93XN8; 1.
DR STRING; 3702.AT3G52340.3; -.
DR iPTMnet; Q93XN8; -.
DR PaxDb; Q93XN8; -.
DR PRIDE; Q93XN8; -.
DR ProteomicsDB; 228292; -. [Q93XN8-1]
DR EnsemblPlants; AT3G52340.1; AT3G52340.1; AT3G52340. [Q93XN8-1]
DR EnsemblPlants; AT3G52340.2; AT3G52340.2; AT3G52340. [Q93XN8-1]
DR EnsemblPlants; AT3G52340.3; AT3G52340.3; AT3G52340. [Q93XN8-1]
DR EnsemblPlants; AT3G52340.7; AT3G52340.7; AT3G52340. [Q93XN8-1]
DR GeneID; 824399; -.
DR Gramene; AT3G52340.1; AT3G52340.1; AT3G52340. [Q93XN8-1]
DR Gramene; AT3G52340.2; AT3G52340.2; AT3G52340. [Q93XN8-1]
DR Gramene; AT3G52340.3; AT3G52340.3; AT3G52340. [Q93XN8-1]
DR Gramene; AT3G52340.7; AT3G52340.7; AT3G52340. [Q93XN8-1]
DR KEGG; ath:AT3G52340; -.
DR Araport; AT3G52340; -.
DR TAIR; locus:2100544; AT3G52340.
DR HOGENOM; CLU_030534_1_0_1; -.
DR InParanoid; Q93XN8; -.
DR OMA; NTDKWNR; -.
DR PhylomeDB; Q93XN8; -.
DR BRENDA; 3.1.3.24; 399.
DR UniPathway; UPA00371; UER00546.
DR PRO; PR:Q93XN8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93XN8; baseline and differential.
DR Genevisible; Q93XN8; AT.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050307; F:sucrose-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR013679; SPP_C.
DR InterPro; IPR006380; SPP_N.
DR InterPro; IPR012847; Sucrose_phosphatase_pln/cyn.
DR Pfam; PF05116; S6PP; 1.
DR Pfam; PF08472; S6PP_C; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR01485; SPP_plant-cyano; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..423
FT /note="Probable sucrose-phosphatase 3b"
FT /id="PRO_0000350616"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_035433"
FT VAR_SEQ 152..155
FT /note="EKRG -> MKVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_035434"
SQ SEQUENCE 423 AA; 48678 MW; 51F409F48C0A4F38 CRC64;
MERLISHPPL MIVSDLDHTM VDHQDHENLS LLRFNSLWEY AYRRDSLLVF STARSPVLYK
ELRKEKPLLT PDIIITSIGT EIAFGNSMVP DHAWVESLNS CKWNREIVLE ETSKFPELTL
QPKTEQRLHK VSFYIDEGKG EALTKELSQL LEKRGLDVKI IYSWGKNVDV IPRGAGKGEA
LEYLLKKLQA EGIFPVNTLA CGDSEHDAEL FSIPDVHGVM VSNSQEELLK WRSENALNNL
KVIHSTERCA DGIIQAIGHF NLGPDLSPRD VSEFLDRKMD NVNPGHEVVR FYLFYERLRR
GEIKNYETYI ASFKDSCLHA AVLFHPSGAE KSLRDTIDEL KKCYGDKRGK KFWVWVDQVL
VTDTIPGKWI VKFDKWEQCE DESQCCKTTV EFTSKGGDLV WEKVKQIWSE ESKVKDDNSS
WIL
