ID H1VX75_COLHI Unreviewed; 585 AA.
AC H1VX75;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=pectinesterase {ECO:0000256|ARBA:ARBA00013229};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229};
DE Flags: Fragment;
GN ORFNames=CH063_14109 {ECO:0000313|EMBL:CCF44837.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF44837.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001440};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361173}.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000256|ARBA:ARBA00010980, ECO:0000256|RuleBase:RU361173}.
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DR EMBL; CACQ02007217; CCF44837.1; -; Genomic_DNA.
DR STRING; 759273.H1VX75; -.
DR EnsemblFungi; CCF44837; CCF44837; CH063_14109.
DR VEuPathDB; FungiDB:CH63R_09225; -.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR HOGENOM; CLU_394823_0_0_1; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
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; 2.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF125; PECTINESTERASE A; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SMART; SM00656; Amb_all; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361173};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361173};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361173};
KW Secreted {ECO:0000256|RuleBase:RU361173};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..585
FT /note="pectinesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003555471"
FT DOMAIN 404..565
FT /note="Pectate lyase"
FT /evidence="ECO:0000259|SMART:SM00656"
FT REGION 353..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..570
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
FT NON_TER 585
FT /evidence="ECO:0000313|EMBL:CCF44837.1"
SQ SEQUENCE 585 AA; 61086 MW; 3860328DA8071EFD CRC64;
MFASSLLLLS SLVAGALGAA RTSPPSGALV VAKSGGTYTS VQKAVDAAKA GGVIFIQPGT
YNEQVLIPAN KGALTIYGYT DDDQDYAKNQ VTITHSLGAD VAGSNDASGT LRAKNDGLRV
YNVNIVNSRG KGVQAIALSA YGNQQGYYGI QAKGYQDTVL SSQGAHYFHA SYVEGATDFI
FGQKAIAWFE ACTLAISGKG YITASGRDAE SNPSWYVINK STVKALSGVG DGQTFLGRPW
RTFARVVFQN SNLGAVVNAA GWSKWGSNPT DNVFYREFAN TGKGASGTRA SFSKKLXAAV
KIADVLGSTS WIDTKYTGXA GXASSSGSGS AAVSKPAVSA DAAESKATPT TLKTVVKASS
TPTPAPDAGA GAGTGSGAGA GAADDCSGTA DGFASLNGGT TGGKGGEVVV VKTQADLEKY
AGASGKHVIK VSGKITITPK GKEVKVSSDK TIVGIGATAE IDQGGFNLQN QRNVIFRNIR
IGNTYVEGDD EGKTQDFDGI QMDNCTNIWI DHVHFEKGGD GLLDSRKDTT FLTVSWTIFR
NHNKAFGIEE EEEEEEEEEE EEEEEEEELA KFMFNADTAD ELDGK
//
