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PLY8_ARATH
ID   PLY8_ARATH              Reviewed;         416 AA.
AC   Q9M8Z8; Q8LF66;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable pectate lyase 8;
DE            EC=4.2.2.2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g07010; ORFNames=F17A9.16;
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=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   [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].
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}.
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DR   EMBL; AC016827; AAF27005.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74488.1; -; Genomic_DNA.
DR   EMBL; AY085026; AAM61584.1; -; mRNA.
DR   RefSeq; NP_187357.1; NM_111581.3.
DR   AlphaFoldDB; Q9M8Z8; -.
DR   SMR; Q9M8Z8; -.
DR   BioGRID; 5221; 1.
DR   STRING; 3702.AT3G07010.1; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   iPTMnet; Q9M8Z8; -.
DR   PaxDb; Q9M8Z8; -.
DR   PRIDE; Q9M8Z8; -.
DR   ProteomicsDB; 234976; -.
DR   EnsemblPlants; AT3G07010.1; AT3G07010.1; AT3G07010.
DR   GeneID; 819886; -.
DR   Gramene; AT3G07010.1; AT3G07010.1; AT3G07010.
DR   KEGG; ath:AT3G07010; -.
DR   Araport; AT3G07010; -.
DR   TAIR; locus:2077622; AT3G07010.
DR   eggNOG; ENOG502QQ5F; Eukaryota.
DR   HOGENOM; CLU_026608_0_1_1; -.
DR   InParanoid; Q9M8Z8; -.
DR   OrthoDB; 582220at2759; -.
DR   PhylomeDB; Q9M8Z8; -.
DR   BioCyc; ARA:AT3G07010-MON; -.
DR   UniPathway; UPA00545; UER00824.
DR   PRO; PR:Q9M8Z8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M8Z8; baseline and differential.
DR   Genevisible; Q9M8Z8; AT.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..416
FT                   /note="Probable pectate lyase 8"
FT                   /id="PRO_0000024872"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000255"
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        17
FT                   /note="A -> T (in Ref. 3; AAM61584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="G -> C (in Ref. 3; AAM61584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="A -> S (in Ref. 3; AAM61584)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   416 AA;  46174 MW;  27BBCB0FB6B047C2 CRC64;
     MAVTKLILFA SALLLTALFI GVNASRSNET WHEHAVENPD EVAAMVDMSI RNSTERRRLG
     YFSCATGNPI DDCWRCDRKW QLRRKRLADC SIGFGRNAIG GRDGRFYVVT DPGDDDPVNP
     IPGTLRHAVI QDEPLWIIFK RDMVITLKQE LIMNSFKTID GRGVNVHIAN GACLTIQYVT
     NIIVHGIHVH DCKPTGNAMV RSSPSHYGFR SMADGDAISI FGSSHIWIDH NSLSNCADGL
     VDAVMSSTAI TVSNNFFTHH NEVMLLGHSD SYTRDKVMQV TIAYNHFGEG LIQRMPRCRH
     GYFHVVNNDY THWEMYAIGG SAGPTINSQG NRFLAPVNPF AKEVTKREYT GESKWKHWNW
     RSEGDLFLNG AFFTRSGAGA GANYARASSL SAKSSSLVGT MTSYSGALNC RAGRRC
 
 
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