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}.
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; 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
//