ID   E1XUM0_AMBAR            Unreviewed;       397 AA.
AC   E1XUM0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Pectate lyase {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU361123};
DE            EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU361123};
GN   Name=amba2.01 {ECO:0000313|EMBL:CBW30994.1};
OS   Ambrosia artemisiifolia (Common ragweed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Ambrosia.
OX   NCBI_TaxID=4212 {ECO:0000313|EMBL:CBW30994.1};
RN   [1] {ECO:0000313|EMBL:CBW30994.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nandy A., Mitulski L.;
RT   "Isoform analysis of Amb a 1 and Amb a 2.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has pectate lyase activity. {ECO:0000256|ARBA:ARBA00002799}.
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         Evidence={ECO:0000256|ARBA:ARBA00000695,
CC         ECO:0000256|RuleBase:RU361123};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU361123};
CC       Note=Binds 1 Ca(2+) ion. Required for its activity.
CC       {ECO:0000256|RuleBase:RU361123};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 2/5. {ECO:0000256|ARBA:ARBA00005220,
CC       ECO:0000256|RuleBase:RU361123}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family. Amb a
CC       subfamily. {ECO:0000256|ARBA:ARBA00008800}.
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DR   EMBL; FR669665; CBW30994.1; -; mRNA.
DR   AlphaFoldDB; E1XUM0; -.
DR   Allergome; 24; Amb a 1.
DR   UniPathway; UPA00545; UER00824.
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; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR018082; AmbAllergen.
DR   InterPro; IPR006626; PbH1.
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:SF159; PECTATE LYASE; 1.
DR   PANTHER; PTHR31683; PECTATE LYASE 18-RELATED; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   PRINTS; PR00807; AMBALLERGEN.
DR   SMART; SM00656; Amb_all; 1.
DR   SMART; SM00710; PbH1; 3.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361123};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361123};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361123}; Signal {ECO:0000256|RuleBase:RU361123}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU361123"
FT   CHAIN           23..397
FT                   /note="Pectate lyase"
FT                   /evidence="ECO:0000256|RuleBase:RU361123"
FT                   /id="PRO_5005127644"
FT   DOMAIN          123..319
FT                   /note="Pectate lyase"
FT                   /evidence="ECO:0000259|SMART:SM00656"
SQ   SEQUENCE   397 AA;  44083 MW;  F0E4BFE1ABA6B414 CRC64;
     MGIKHCCYIL YFTLALVTLV QAGRLGEEVD ILPSPNDTRR SLQGCEAHNI IDKCWRCKPD
     WAENRQALGD CAQGFGKATH GGKWGDIYMV TSDQDDDVVN PKEGTLRFGA TQDRPLWIIF
     QRDMIIYLQQ EMVVTSDKTI DGRGAKVELV YGGITLMNVK NVIIHNIDIH DVRVLPGGRI
     KSNGGPAIPR HQSDGDAIHV TGSSDIWIDH CTLSKSFDGL VDVNWGSTGV TISNCKFTHH
     EKAVLLGASD THFQDLKMHV TLAYNIFTNT VHERMPRCRF GFFQIVNNFY DRWDKYAIGG
     SSNPTILSQG NKFVAPDFIY KKNVCLRTGA QEPEWMTWNW RTQNDVLENG AIFVASGSDP
     VLTAEQNAGM MQAEPGDMVP QLTMNAGVLT CSPGAPC
//