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Database: UniProt
Entry: A0A0K9NME2_ZOSMR
LinkDB: A0A0K9NME2_ZOSMR
Original site: A0A0K9NME2_ZOSMR 
ID   A0A0K9NME2_ZOSMR        Unreviewed;       349 AA.
AC   A0A0K9NME2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=pectinesterase {ECO:0000256|ARBA:ARBA00013229};
DE            EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229};
GN   ORFNames=ZOSMA_80G00510 {ECO:0000313|EMBL:KMZ57958.1}, ZOSMA_80G00520
GN   {ECO:0000313|EMBL:KMZ57959.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ57959.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|EMBL:KMZ57959.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Finnish {ECO:0000313|EMBL:KMZ57959.1};
RA   Olsen J.L., Schmutz J., Jenkins J., Grimwood J., Amirebrahimi M., Tice H.,
RA   Chovatia M., Van de Peer Y., Rouze P., Verhelst B., Lin Y.-C.;
RT   "The genome of the seagrass Zostera marina.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}.
CC   -!- SIMILARITY: Belongs to the pectinesterase family.
CC       {ECO:0000256|ARBA:ARBA00008891}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMZ57959.1}.
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DR   EMBL; LFYR01001997; KMZ57958.1; -; Genomic_DNA.
DR   EMBL; LFYR01001997; KMZ57959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9NME2; -.
DR   STRING; 29655.A0A0K9NME2; -.
DR   OMA; LGRHHFS; -.
DR   OrthoDB; 668039at2759; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IBA:GO_Central.
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; IPR000070; Pectinesterase_cat.
DR   PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR   PANTHER; PTHR31321:SF76; PECTINESTERASE 29-RELATED; 1.
DR   Pfam; PF01095; Pectinesterase; 2.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..349
FT                   /note="pectinesterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014030309"
FT   DOMAIN          30..115
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
FT   DOMAIN          132..340
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
SQ   SEQUENCE   349 AA;  39656 MW;  28E197AAE222DCD5 CRC64;
     MTLTFHFIMG FLGFLWISFA LSPEDFRKTI IVGKNGQTPF KTVQSAIDSI PNDNLQWIKI
     HIQAGTFREQ VRIPRNKGFI LLEGEGRDKT TLVESKYINV ETWNLNRTTR FEKGFITDMD
     EYQKINLDAL EDSATFVSEA NNIIVKDITL KNDYSSSTGL IKRAVAADIK GDMTSFYNCG
     FVSFQDTLYD RSGRHYFSNC YIEGHVDYIF GHGQSIYERC TIFSATNKKG SKGWITAQGR
     AKSTDPDGFL FKDCDLTGPG LSYLGRAWGS YSKVVFYRSK MANIIVPEGW DQWDQSPSNL
     EYSEYDCSGP GSSLSSRVNW MKTLSSKEIE LYSGNLFIDN QGWINDQPK
//
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