ID I1CUM9_RHIO9 Unreviewed; 339 AA.
AC I1CUM9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Pectinesterase {ECO:0000256|ARBA:ARBA00013229, ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229, ECO:0000256|RuleBase:RU000589};
GN ORFNames=RO3G_16870 {ECO:0000313|EMBL:EIE92159.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE92159.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE92159.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
CC -!- FUNCTION: Involved in maceration and soft-rotting of plant tissue.
CC {ECO:0000256|RuleBase:RU000589}.
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 ECO:0000256|RuleBase:RU000589};
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184,
CC ECO:0000256|RuleBase:RU000589}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU000589}.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR EMBL; CH476754; EIE92159.1; -; Genomic_DNA.
DR AlphaFoldDB; I1CUM9; -.
DR STRING; 246409.I1CUM9; -.
DR VEuPathDB; FungiDB:RO3G_16870; -.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR InParanoid; I1CUM9; -.
DR OMA; NEGRQIY; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
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:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW ECO:0000256|RuleBase:RU000589};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU000589};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW Secreted {ECO:0000256|RuleBase:RU000589};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU000589}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT CHAIN 22..339
FT /note="Pectinesterase"
FT /evidence="ECO:0000256|RuleBase:RU000589"
FT /id="PRO_5005134871"
FT DOMAIN 30..328
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 339 AA; 37376 MW; 44569E04F53AA8E3 CRC64;
MRLSLGQILI PSSLLVSLAN AVSTTLHVCS SCDYTNITSA LNALPNTTET WTVAIAPGNY
KEKIILTRSN VILKPSSSKG KVSIQYDSFK DTQSHVGKDS DAAVLAVRGQ NVKVYDMTIA
NVFHQTRNMA NLALSVEAKQ VSFYGVKFYG FQDTLYVTKN STAYFKNCHV EGSVDFIFGS
GVGYFEDCEI ASNMNGGYIT AHKRSSADAE GGLYFNNCKA FATLPSGPLA DTKNTSMSFT
SSSQFPNSCY LGRPWNQHAR VVFMNSEIGS HIKPAAWSVW QAKDPRTDGV AFYEYNNGGN
NPWNASIRAN FSSLLTKSEA KQYTLKNVFK HYSWIDSRY
//
