GenomeNet

Database: UniProt
Entry: U7PXD0_SPOS1
LinkDB: U7PXD0_SPOS1
Original site: U7PXD0_SPOS1 
ID   U7PXD0_SPOS1            Unreviewed;       326 AA.
AC   U7PXD0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   03-MAY-2023, entry version 41.
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=HMPREF1624_03629 {ECO:0000313|EMBL:ERT00258.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT00258.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
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}.
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; KI440844; ERT00258.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PXD0; -.
DR   STRING; 1391915.U7PXD0; -.
DR   eggNOG; ENOG502QSQ4; Eukaryota.
DR   HOGENOM; CLU_012243_1_0_1; -.
DR   OrthoDB; 668039at2759; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000018087; 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:SF127; PECTINESTERASE; 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:UP000018087};
KW   Secreted {ECO:0000256|RuleBase:RU000589};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU000589}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT   CHAIN           17..326
FT                   /note="Pectinesterase"
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT                   /id="PRO_5005148007"
FT   DOMAIN          27..297
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ   SEQUENCE   326 AA;  34118 MW;  248E66BFE11DA83E CRC64;
     MLSTLVLSMC IGHAFATGRT SPPSGSITVC SSGCDYNIIQ KAVGSISPTS KSPSKIFVYA
     GTYTEQVTIP VLAGALTIYG QTANTASYTS NVVNLTWKSS AADGFDDEHT AALINLSPSV
     RIYNINIKNT YGKGSQAIAL AAYNTKQGYY GVGLYGYQDT LLAQTGNQVY AGCYIEGAVD
     FVFGQYARAW ITKSDIALKA GGGSITADGR PSASGDSYYV IDQSTVTAAS GASVASGTVY
     LGRPWSQYAR VCVQKTVLSS IVNAAGWSIW STSTPNTAGV SFQEYDNTGA GARGTRVSLA
     TKLSSPISIG TILDSDYANW VDTSYV
//
DBGET integrated database retrieval system