PLY5_ARATH
ID PLY5_ARATH Reviewed; 408 AA.
AC Q9FXD8; Q8L8V9; Q8W116;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable pectate lyase 5;
DE EC=4.2.2.2;
DE Flags: Precursor;
GN OrderedLocusNames=At1g67750; ORFNames=F12A21.12;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-408.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC their non-reducing ends.; EC=4.2.2.2;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. Required for its activity. {ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 2/5.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG28907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008113; AAG28907.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34690.1; -; Genomic_DNA.
DR EMBL; AF462797; AAL58893.1; -; mRNA.
DR EMBL; AY101535; AAM26656.1; -; mRNA.
DR EMBL; AY088778; AAM67091.1; -; mRNA.
DR RefSeq; NP_564906.1; NM_105443.5.
DR AlphaFoldDB; Q9FXD8; -.
DR SMR; Q9FXD8; -.
DR BioGRID; 28321; 1.
DR STRING; 3702.AT1G67750.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PaxDb; Q9FXD8; -.
DR PRIDE; Q9FXD8; -.
DR ProteomicsDB; 226204; -.
DR EnsemblPlants; AT1G67750.1; AT1G67750.1; AT1G67750.
DR GeneID; 843100; -.
DR Gramene; AT1G67750.1; AT1G67750.1; AT1G67750.
DR KEGG; ath:AT1G67750; -.
DR Araport; AT1G67750; -.
DR TAIR; locus:2008550; AT1G67750.
DR eggNOG; ENOG502QQ5F; Eukaryota.
DR HOGENOM; CLU_026608_0_1_1; -.
DR InParanoid; Q9FXD8; -.
DR OMA; KEWSKWN; -.
DR OrthoDB; 924221at2759; -.
DR PhylomeDB; Q9FXD8; -.
DR BioCyc; ARA:AT1G67750-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:Q9FXD8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXD8; baseline and differential.
DR Genevisible; Q9FXD8; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR018082; AmbAllergen.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR PANTHER; PTHR31683; PTHR31683; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR PRINTS; PR00807; AMBALLERGEN.
DR SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 2: Evidence at transcript level;
KW Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..408
FT /note="Probable pectate lyase 5"
FT /id="PRO_0000024869"
FT ACT_SITE 286
FT /evidence="ECO:0000255"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 47
FT /note="S -> A (in Ref. 4; AAM67091)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="R -> L (in Ref. 4; AAM67091)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="G -> A (in Ref. 4; AAM67091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 44886 MW; B44DCF15C8B8E69B CRC64;
MRMTLVHLSL SLFSCLLLVL SPTFIASTPV SEPELVVQEV NEKINASRRN LGVLSCGTGN
PIDDCWRCDP KWEKNRQRLA DCAIGFGKHA IGGRDGKIYV VTDSSDKDVV NPKPGTLRHA
VIQDEPLWII FARDMVIKLK EELIMNSFKT IDGRGASVHI AGGACITVQY VTNIIIHGVN
IHDCKRKGNA YVRDSPSHYG WRTASDGDAV SIFGGSHVWV DHCSLSNCAD GLIDAIHGST
AITISNNYLS HHNKVMLLGH SDSYTRDKNM QVTIAFNHFG EGLVQRMPRC RHGYFHVVNN
DYTHWQMYAI GGSAAPTINS QGNRFLAPND HVFKEVTKYE DAPRSKWKKW NWRSEGDLFL
NGAFFTPSGG GASSSYAKAS SLSARPSSLV ASVTSNAGAL FCRKGSRC
