PTLY_THEMA
ID PTLY_THEMA Reviewed; 367 AA.
AC Q9WYR4;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pectate trisaccharide-lyase;
DE EC=4.2.2.22;
DE AltName: Full=Pectate lyase A {ECO:0000303|PubMed:12443532, ECO:0000312|EMBL:AAD35518.1};
DE Short=PelA {ECO:0000303|PubMed:12443532};
DE Flags: Precursor;
GN Name=pelA {ECO:0000303|PubMed:12443532}; OrderedLocusNames=TM_0433;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1] {ECO:0000312|EMBL:AAD35518.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000269|PubMed:12443532};
RX PubMed=12443532; DOI=10.1042/bj20021595;
RA Kluskens L.D., van Alebeek G.J., Voragen A.G., de Vos W.M.,
RA van der Oost J.;
RT "Molecular and biochemical characterization of the thermoactive family 1
RT pectate lyase from the hyperthermophilic bacterium Thermotoga maritima.";
RL Biochem. J. 370:651-659(2003).
CC -!- FUNCTION: Cleaves unsaturated trigalacturonate from pectin. Activity is
CC highest towards polygalacturonic acid, activity on methylated pectins
CC decreases with an increasing degree of methylation.
CC {ECO:0000269|PubMed:12443532}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eliminative cleavage of unsaturated trigalacturonate as the
CC major product from the reducing end of polygalacturonic
CC acid/pectate.; EC=4.2.2.22; Evidence={ECO:0000269|PubMed:12443532};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12443532};
CC -!- ACTIVITY REGULATION: Completely inactivated by EGTA.
CC {ECO:0000269|PubMed:12443532}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for polygalacturonic acid {ECO:0000269|PubMed:12443532};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:12443532};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. Half-life in the presence
CC of 0.6 mM CaCl(2) is 110 minutes at 95 degrees Celsius and 15 minutes
CC at 100 degrees Celsius. Half-life in the absence of CaCl(2) is 5
CC minutes at 90 degrees Celsius. {ECO:0000269|PubMed:12443532};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12443532}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12443532}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000255}.
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DR EMBL; AE000512; AAD35518.1; -; Genomic_DNA.
DR PIR; D72376; D72376.
DR RefSeq; NP_228243.1; NC_000853.1.
DR RefSeq; WP_010865117.1; NC_023151.1.
DR PDB; 3ZSC; X-ray; 1.94 A; A=28-367.
DR PDBsum; 3ZSC; -.
DR AlphaFoldDB; Q9WYR4; -.
DR SMR; Q9WYR4; -.
DR STRING; 243274.THEMA_02560; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR PRIDE; Q9WYR4; -.
DR EnsemblBacteria; AAD35518; AAD35518; TM_0433.
DR KEGG; tma:TM0433; -.
DR PATRIC; fig|243274.5.peg.439; -.
DR eggNOG; COG3866; Bacteria.
DR InParanoid; Q9WYR4; -.
DR OMA; HQHVYNN; -.
DR BioCyc; MetaCyc:MON-17962; -.
DR BRENDA; 4.2.2.2; 6331.
DR BRENDA; 4.2.2.22; 6331.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
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 SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism;
KW Cell wall biogenesis/degradation; Lyase; Metal-binding;
KW Polysaccharide degradation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..367
FT /note="Pectate trisaccharide-lyase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000405016"
FT REPEAT 151..173
FT /note="PbH1 1"
FT /evidence="ECO:0000255"
FT REPEAT 263..289
FT /note="PbH1 2"
FT /evidence="ECO:0000255"
FT ACT_SITE 224
FT /evidence="ECO:0000250|UniProtKB:P39116"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P39116"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P39116"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P39116"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3ZSC"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:3ZSC"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 75..93
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 95..116
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3ZSC"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3ZSC"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:3ZSC"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:3ZSC"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3ZSC"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:3ZSC"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:3ZSC"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3ZSC"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:3ZSC"
SQ SEQUENCE 367 AA; 40607 MW; FDF57647B8476195 CRC64;
MLMRFSRVVS LVLLLVFTAV LTGAVKASLN DKPVGFASVP TADLPEGTVG GLGGEIVFVR
TAEELEKYTT AEGKYVIVVD GTIVFEPKRE IKVLSDKTIV GINDAKIVGG GLVIKDAQNV
IIRNIHFEGF YMEDDPRGKK YDFDYINVEN SHHIWIDHCT FVNGNDGAVD IKKYSNYITV
SWCKFVDHDK VSLVGSSDKE DPEQAGQAYK VTYHHNYFKN CIQRMPRIRF GMAHVFNNFY
SMGLRTGVSG NVFPIYGVAS AMGAKVHVEG NYFMGYGAVM AEAGIAFLPT RIMGPVEGYL
TLGEGDAKNE FYYCKEPEVR PVEEGKPALD PREYYDYTLD PVQDVPKIVV DGAGAGKLVF
EELNTAQ
