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Database: UniProt
Entry: B9FYC2_ORYSJ
LinkDB: B9FYC2_ORYSJ
Original site: B9FYC2_ORYSJ 
ID   B9FYC2_ORYSJ            Unreviewed;       398 AA.
AC   B9FYC2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
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=OsJ_25062 {ECO:0000313|EMBL:EEE67559.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:EEE67559.1};
RN   [1] {ECO:0000313|EMBL:EEE67559.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [2] {ECO:0000313|EMBL:EEE67559.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang J., Li R., Fan W., Huang Q., Zhang J., Zhou Y., Hu Y., Zi S., Li J.,
RA   Ni P., Zheng H., Zhang Y., Zhao M., Hao Q., McDermott J., Samudrala R.,
RA   Kristiansen K., Wong G.K.-S.;
RT   "Improved gene annotation of the rice (Oryza sativa) genomes.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the pectinesterase family.
CC       {ECO:0000256|ARBA:ARBA00008891}.
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DR   EMBL; CM000144; EEE67559.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9FYC2; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000007752; Chromosome 7.
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:SF31; PECTINESTERASE QRT1; 1.
DR   Pfam; PF01095; Pectinesterase; 2.
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}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW   Signal {ECO:0000256|RuleBase:RU000589}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT   CHAIN           17..398
FT                   /note="Pectinesterase"
FT                   /evidence="ECO:0000256|RuleBase:RU000589"
FT                   /id="PRO_5005124192"
FT   DOMAIN          75..259
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
FT   DOMAIN          282..392
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
FT   REGION          45..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ   SEQUENCE   398 AA;  41976 MW;  982AA0E57186B058 CRC64;
     MAATGVLVVV VALVFAVTVA GGGGAGVGGD GGFITWEDLS MPAGAARSST WDDTAGGGGG
     KRSGGGGGGE QRTTIVVSPD GTGHSRTVQG AVDMVPAGNT RRVKIVVRPG VYREKVTVPI
     TKPFVSLIGM GTGHTVITWH SRASDVGASG HQVGTFYSAS VAVEADYFCA SHITFENSAA
     AAAPGAVGQQ AVALRLSGDK TVLYKCRILG TQDTLFDNIG RHYLYNCDIQ GSIDFIFGNA
     RSLYQSCHKL TIQAFTNSSI LYLTAKELLT LGCTLHAVAT SYGAIAASQR SSPSEESGFS
     FVGCRLTGSG MLYLGRAWGK YSRVVYSYCD LSGIIVPQGW SDWGDQSRTK TVLFGEYNCK
     GPGASTKQRV PWSRTLTYDE ARPFIGRSFI NGEQWLRL
//
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