PLY12_ARATH
ID PLY12_ARATH Reviewed; 483 AA.
AC Q9SCP2; Q8LFH8;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable pectate lyase 12;
DE EC=4.2.2.2;
DE Flags: Precursor;
GN OrderedLocusNames=At3g53190; ORFNames=T4D2.120;
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61400.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB64222.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL132958; CAB64222.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79046.1; -; Genomic_DNA.
DR EMBL; AY084835; AAM61400.1; ALT_INIT; mRNA.
DR PIR; T46165; T46165.
DR RefSeq; NP_566979.1; NM_115179.5.
DR AlphaFoldDB; Q9SCP2; -.
DR SMR; Q9SCP2; -.
DR BioGRID; 9802; 16.
DR IntAct; Q9SCP2; 15.
DR STRING; 3702.AT3G53190.1; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PaxDb; Q9SCP2; -.
DR PRIDE; Q9SCP2; -.
DR ProteomicsDB; 234937; -.
DR EnsemblPlants; AT3G53190.1; AT3G53190.1; AT3G53190.
DR GeneID; 824485; -.
DR Gramene; AT3G53190.1; AT3G53190.1; AT3G53190.
DR KEGG; ath:AT3G53190; -.
DR Araport; AT3G53190; -.
DR TAIR; locus:2101998; AT3G53190.
DR eggNOG; ENOG502QPY9; Eukaryota.
DR HOGENOM; CLU_026608_0_0_1; -.
DR InParanoid; Q9SCP2; -.
DR OMA; ANMEIKL; -.
DR OrthoDB; 924221at2759; -.
DR PhylomeDB; Q9SCP2; -.
DR BioCyc; ARA:AT3G53190-MON; -.
DR UniPathway; UPA00545; UER00824.
DR PRO; PR:Q9SCP2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCP2; baseline and differential.
DR Genevisible; Q9SCP2; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS: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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..483
FT /note="Probable pectate lyase 12"
FT /id="PRO_0000024876"
FT ACT_SITE 300
FT /evidence="ECO:0000255"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 17
FT /note="L -> F (in Ref. 3; AAM61400)"
FT /evidence="ECO:0000305"
FT CONFLICT 21..22
FT /note="MV -> KG (in Ref. 3; AAM61400)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="M -> I (in Ref. 3; AAM61400)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="R -> T (in Ref. 3; AAM61400)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="I -> V (in Ref. 3; AAM61400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 53593 MW; 5A1FC9726BBA5190 CRC64;
MMLQRSCIVL FFSLFLLVPQ MVFSMLNRTL LLIPHPDPEL VAYQVQWKVN ASITRRQALD
TTDQAGSTPC ITGNPIDDCW KCDPNWPNNR QGLADCGIGF GQYALGGKGG QFYFVTDSSD
DDAVNPKPGT LRYGVIQEEP LWIVFPSNMM IKLKQELIFN SYKTLDGRGA NVHIVGGGCI
TLQYVSNIII HNIHIHHCYQ SGNTNVRSSP THYGFRTKSD GDGISIFGSK DIWIDHCSLS
RCKDGLIDAV MGSTGITISN NFFSHHNEVM LLGHSDHYEP DSGMQVTIAF NHFGEKLIQR
MPRCRRGYIH VVNNDFTQWE MYAIGGSGNP TINSQGNRYT APTNPFAKEV TKRVETPDGD
WKGWNWRSEG DILVNGAFFV ASGEGAEMRY EKAYSVEPKS ASFITQITFH SGVLGVGGRN
NNLGMWTTTG SEGTSGLDSY NDYTDEMSGA GSTNRLSFSV LVFLLSSISY LVVFTSSTQM
FML
