ID PLYL_EMENI Reviewed; 410 AA. AC Q5BA93; C8VPM0; DT 22-FEB-2023, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 24-JAN-2024, entry version 99. DE RecName: Full=Pectate lyase PEL9 {ECO:0000303|PubMed:35802235}; DE EC=4.2.2.2 {ECO:0000269|PubMed:35802235}; DE AltName: Full=AnPL9 {ECO:0000303|PubMed:35802235}; DE Flags: Precursor; GN Name=PEL9 {ECO:0000305}; Synonyms=PL9 {ECO:0000303|PubMed:35802235}; GN ORFNames=ANIA_02537 {ECO:0000312|EMBL:CBF87052.1}; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / OS M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Nidulantes. OX NCBI_TaxID=227321 {ECO:0000312|Proteomes:UP000000560}; RN [1] {ECO:0000312|Proteomes:UP000000560} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). RN [2] {ECO:0000312|Proteomes:UP000000560} RP GENOME REANNOTATION. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139 RC {ECO:0000312|Proteomes:UP000000560}; RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003; RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K., RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J., RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., RA Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a community RT effort."; RL Fungal Genet. Biol. 46:S2-13(2009). RN [3] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION. RC STRAIN=A26 {ECO:0000303|PubMed:35802235}; RX PubMed=35802235; DOI=10.1007/s12010-022-04036-x; RA Suzuki H., Morishima T., Handa A., Tsukagoshi H., Kato M., Shimizu M.; RT "Biochemical Characterization of a Pectate Lyase AnPL9 from Aspergillus RT nidulans."; RL Appl. Biochem. Biotechnol. 0:0-0(2022). CC -!- FUNCTION: Presents an endo-cleaving activity on the homogalacturonan CC (HG) region in pectin (PubMed:35802235). Active on homogalacturonan CC with a degree of polymerization above 4, and does not appear to be CC affected by the degree of methylation of the substrate CC (PubMed:35802235). Does not degrade linear rhamnogalacturonan CC (PubMed:35802235). {ECO:0000269|PubMed:35802235}. 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:0000269|PubMed:35802235}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000305|PubMed:35802235}; CC -!- ACTIVITY REGULATION: Inhibited by iron ions (PubMed:35802235). CC Activated in presence of the surfactant polysorbate 20, while inhibited CC in the presence of Triton X-100 and sodium dodecyl sulfate CC (PubMed:35802235). Inhibited in presence of the organic solvents CC methanol, ethanol, propan-2-ol and acetone (PubMed:35802235). CC {ECO:0000269|PubMed:35802235}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Note=kcat is 280 sec(-1) for homogalacturonan (HG) (at 45 degrees CC Celsius and at pH 8) (PubMed:35802235). kcat is 357 sec(-1) for apple CC pectin (at 45 degrees Celsius and at pH 8) (PubMed:35802235). kcat is CC 272 sec(-1) for citrus peel pectin (at 45 degrees Celsius and at pH CC 8) (PubMed:35802235). kcat is 236 sec(-1) for rhamnogalacturonan type CC I (at 45 degrees Celsius and at pH 8) (PubMed:35802235). CC {ECO:0000269|PubMed:35802235}; CC pH dependence: CC Optimum pH is 8. {ECO:0000269|PubMed:35802235}; CC Temperature dependence: CC Optimum temperature is 45 degrees Celsius. CC {ECO:0000269|PubMed:35802235}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:35802235}. CC -!- INDUCTION: Induced during growth on homogalacturonan (HG). CC {ECO:0000269|PubMed:35802235}. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 9 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BN001307; CBF87052.1; -; Genomic_DNA. DR RefSeq; XP_660141.1; XM_655049.1. DR AlphaFoldDB; Q5BA93; -. DR SMR; Q5BA93; -. DR STRING; 227321.Q5BA93; -. DR CAZy; PL9; Polysaccharide Lyase Family 9. DR EnsemblFungi; CBF87052; CBF87052; ANIA_02537. DR GeneID; 2874771; -. DR KEGG; ani:AN2537.2; -. DR VEuPathDB; FungiDB:AN2537; -. DR eggNOG; ENOG502QSUT; Eukaryota. DR HOGENOM; CLU_030634_1_0_1; -. DR InParanoid; Q5BA93; -. DR OMA; DSHHNYD; -. DR OrthoDB; 2292519at2759; -. DR Proteomes; UP000000560; Chromosome VII. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030570; F:pectate lyase activity; IDA:UniProtKB. DR GO; GO:0052009; P:symbiont-mediated disruption of host cell wall; IDA:UniProtKB. DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1. DR InterPro; IPR039448; Beta_helix. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1. DR PANTHER; PTHR40088:SF1; PECTATE LYASE (EUROFUNG); 1. DR Pfam; PF13229; Beta_helix; 1. DR SUPFAM; SSF51126; Pectin lyase-like; 1. PE 1: Evidence at protein level; KW Calcium; Glycoprotein; Lyase; Metal-binding; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..410 FT /note="Pectate lyase PEL9" FT /evidence="ECO:0000255" FT /id="PRO_5010168540" FT REGION 342..361 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 381..410 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 271 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P0C1A7" FT BINDING 191 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P0C1A7" FT BINDING 215 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P0C1A7" FT BINDING 216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P0C1A7" FT BINDING 219 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P0C1A7" FT CARBOHYD 234 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" SQ SEQUENCE 410 AA; 43891 MW; 1BF619F86AB51CE6 CRC64; MMGKSVWVFA ALFPAVLAAD IYVSPDGSDD AAGTIDAPLQ SIQLAVDQAT AGSTIYLRGG TYTPTSNIQI TKSGTASAPY VLRAYEGESV IIDGEELPGT PADLDASLDN ADRGILHIQD AEYWEFYDLE LINGPYGVYA RDASNNHYER ITTRNNYETG FQLQGESSNN VVLYLDSYGN RDPRKNGESA DGFACKEGSG EGNILRGARL WNNVDDGLDL WYAVNPVHPR ISANTSREFK SAVTIEDTIA WGNGFNRWDF TPFEGDGNGF KLGGGDDTDI GPADHIITNC IAFSNAKDGF TDNSQPGNFV LTRNTAWDNT AVGFKFGTAV ATLTGNIAAS NGEAPTSLSD EQISDGNSWD GDEDWDDGSF VSVDVSLVQG ERNADGTIEP SGFLLPADGE EIGATTDWSA //