GenomeNet

Database: UniProt
Entry: A0A0P0V1X3_ORYSJ
LinkDB: A0A0P0V1X3_ORYSJ
Original site: A0A0P0V1X3_ORYSJ 
ID   A0A0P0V1X3_ORYSJ        Unreviewed;       428 AA.
AC   A0A0P0V1X3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE            EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN   OrderedLocusNames=Os01g0312500 {ECO:0000313|EMBL:BAS71790.1};
GN   ORFNames=OSNPB_010312500 {ECO:0000313|EMBL:BAS71790.1};
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:BAS71790.1, ECO:0000313|Proteomes:UP000059680};
RN   [1] {ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RA   Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA   Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA   Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA   Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA   Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA   Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA   Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA   Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA   Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA   Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA   Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA   Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA   Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA   Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA   Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA   Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA   Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA   Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA   Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA   Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA   Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA   Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA   Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA   Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA   Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA   Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA   Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA   Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA   Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA   Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA   Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA   Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA   Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA   Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA   Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA   Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA   Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA   Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA   Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA   Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2] {ECO:0000313|EMBL:BAS71790.1, ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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|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: In the C-terminal section; belongs to the pectinesterase
CC       family. {ECO:0000256|ARBA:ARBA00007786}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC       {ECO:0000256|ARBA:ARBA00006027}.
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DR   EMBL; AP014957; BAS71790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P0V1X3; -.
DR   SMR; A0A0P0V1X3; -.
DR   STRING; 39947.A0A0P0V1X3; -.
DR   PaxDb; 39947-A0A0P0V1X3; -.
DR   eggNOG; ENOG502QVXG; Eukaryota.
DR   InParanoid; A0A0P0V1X3; -.
DR   OMA; GISVQKC; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000059680; Chromosome 1.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR   GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0042545; P:cell wall modification; IEA:UniProtKB-UniRule.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd15798; PMEI-like_3; 1.
DR   Gene3D; 1.20.140.40; Invertase/pectin methylesterase inhibitor family protein; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR035513; Invertase/methylesterase_inhib.
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   InterPro; IPR006501; Pectinesterase_inhib_dom.
DR   PANTHER; PTHR31707; PECTINESTERASE; 1.
DR   PANTHER; PTHR31707:SF147; PECTINESTERASE_PECTINESTERASE INHIBITOR 40-RELATED; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   Pfam; PF04043; PMEI; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF101148; Plant invertase/pectin methylesterase inhibitor; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
PE   1: Evidence at protein level;
KW   Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085,
KW   ECO:0000256|RuleBase:RU000589}; Hydrolase {ECO:0000256|RuleBase:RU000589};
KW   Proteomics identification {ECO:0007829|ProteomicsDB:A0A0P0V1X3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059680}.
FT   DOMAIN          2..49
FT                   /note="Pectinesterase inhibitor"
FT                   /evidence="ECO:0000259|Pfam:PF04043"
FT   DOMAIN          117..414
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
FT   REGION          51..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAS71790.1"
SQ   SEQUENCE   428 AA;  46385 MW;  B4A2653C4AC0A8FB CRC64;
     HVMTELSAAM TNQYTCLDGF DYKDGERVRH YMESSIHHVS RMVSNSLAMA KKLPGAGGGG
     MTPSSSSPDT ATQSESSETT QRQPFMGYGQ MANGFPKWVR PGDRRLLQAP ASSITPDAVV
     AKDGSGGYTT VSAAVAAAPA NSNKRYVIHI KAGAYMENVE VGKSKKNLMF IGDGIGKTVI
     KASRNVVDGS TTFRSATVAV VGNNFLARDL TIENSAGPSK HQAVALRVGA DLSAFYRCSF
     VGYQDTLYVH SLRQFFRECD IYGTIDFIFG NSAVVFQSCN LYARRPLPNQ SNVYTAQGRE
     DPNQNTGISI QKCKVAAASD LLAVQSSFKT YLGRPWKQYS RTVFMQSELD SVVNPAGWLE
     WSGNFALDTL YYGEYQNTGP GASTSNRVKW KGYRVITSAS EASTFTVGNF IDGDVWLAGT
     SVPFTVGL
//
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