ID Q5ZAW1_ORYSJ Unreviewed; 546 AA.
AC Q5ZAW1; B9ETP3;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Pectinesterase {ECO:0000256|RuleBase:RU000589};
DE EC=3.1.1.11 {ECO:0000256|RuleBase:RU000589};
GN OrderedLocusNames=Os01g0788400 {ECO:0000313|EMBL:BAS74709.1};
GN ORFNames=OSNPB_010788400 {ECO:0000313|EMBL:BAS74709.1};
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:BAS74709.1, ECO:0000313|Proteomes:UP000059680};
RN [1] {ECO:0000313|EMBL:BAH00252.1}
RP NUCLEOTIDE SEQUENCE.
RA Kikuchi S., Satoh K., Nagata T., Kawagashira N., Doi K., Kishimoto N.,
RA Yazaki J., Ishikawa M., Yamada H., Ooka H., Hotta I., Kojima K., Namiki T.,
RA Ohneda E., Yahagi W., Suzuki K., Li C., Ohtsuki K., Shishiki T., Otomo Y.,
RA Murakami K., Iida Y., Sugano S., Fujimura T., Suzuki Y., Tsunoda Y.,
RA Kurosaki T., Kodama T., Masuda H., Kobayashi M., Xie Q., Lu M.,
RA Narikawa R., Sugiyama A., Mizuno K., Yokomizo S., Niikura J., Ikeda R.,
RA Ishibiki J., Kawamata M., Yoshimura A., Miura J., Kusumegi T., Oka M.,
RA Ryu R., Ueda M., Matsubara K., Kawai J., Carninci P., Adachi J., Aizawa K.,
RA Arakawa T., Fukuda S., Hara A., Hashidume W., Hayatsu N., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Kondo S., Konno H., Miyazaki A., Osato N.,
RA Ota Y., Saito R., Sasaki D., Sato K., Shibata K., Shinagawa A., Shiraki T.,
RA Yoshino M., Hayashizaki Y.;
RT "Collection, Mapping, and Annotation of Over 28,000 cDNA Clones from
RT japonica Rice.";
RL Science 301:376-379(2003).
RN [2] {ECO:0000313|EMBL:BAH00252.1}
RP NUCLEOTIDE SEQUENCE.
RA Adachi J., Aizawa K., Akimura T., Arakawa T., Carninci P., Doi K.,
RA Fujimura T., Fukuda S., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA Hayashizaki Y., Hayatsu N., Hiramoto K., Hiraoka T., Hori F., Hotta I.,
RA Iida J., Iida Y., Ikeda R., Imamura K., Imotani K., Ishibiki J., Ishii Y.,
RA Ishikawa M., Itoh M., Kagawa I., Kanagawa S., Katoh H., Kawagashira N.,
RA Kawai J., Kawamata M., Kikuchi S., Kishikawa-Hirozane T., Kishimoto N.,
RA Kobayashi M., Kodama T., Kojima K., Kojima Y., Kondo S., Konno H.,
RA Kouda M., Koya S., Kurihara C., Kurosaki T., Kusumegi T., Li C., Lu M.,
RA Masuda H., Matsubara K., Matsuyama T., Miura J., Miyazaki A., Mizuno K.,
RA Murakami K., Murata M., Nagata T., Nakahama Y., Nakamura M., Namiki T.,
RA Narikawa R., Niikura J., Nishi K., Nomura K., Numasaki R., Ohneda E.,
RA Ohno M., Ohtsuki K., Oka M., Ooka H., Osato N., Ota Y., Otomo Y., Ryu R.,
RA Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H., Sasaki D., Sato K.,
RA Satoh K., Shibata K., Shinagawa A., Shiraki T., Shishiki T., Sogabe Y.,
RA Sugano S., Sugiyama A., Suzuki K., Suzuki Y., Tagami M., Tagami-Takeda Y.,
RA Tagawa A., Takahashi F., Takaku-Akahira S., Tanaka T., Tomaru A., Toya T.,
RA Tsunoda Y., Ueda M., Waki K., Xie Q., Yahagi W., Yamada H., Yamamoto M.,
RA Yasunishi A., Yazaki J., Yokomizo S., Yoshimura A.;
RT "Collection, mapping, and annotation of 28K full-length cDNA clones from
RT japonica rice.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {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 [4] {ECO:0000313|EMBL:BAS74709.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23299411; DOI=10.1093/pcp/pcs183;
RA Sakai H., Lee S.S., Tanaka T., Numa H., Kim J., Kawahara Y., Wakimoto H.,
RA Yang C.C., Iwamoto M., Abe T., Yamada Y., Muto A., Inokuchi H., Ikemura T.,
RA Matsumoto T., Sasaki T., Itoh T.;
RT "Rice Annotation Project Database (RAP-DB): an integrative and interactive
RT database for rice genomics.";
RL Plant Cell Physiol. 54:E6-E6(2013).
RN [5] {ECO:0000313|EMBL:BAS74709.1, 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).
RN [6] {ECO:0000313|EMBL:BAS74709.1}
RP NUCLEOTIDE SEQUENCE.
RA Sakai H., Kawahara Y., Matsumoto T., Buell C.R., Itoh T.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin.
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|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, cell wall
CC {ECO:0000256|ARBA:ARBA00004191, 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; AK120977; BAH00252.1; -; mRNA.
DR EMBL; AP014957; BAS74709.1; -; Genomic_DNA.
DR RefSeq; XP_015621142.1; XM_015765656.1.
DR AlphaFoldDB; Q5ZAW1; -.
DR SMR; Q5ZAW1; -.
DR STRING; 39947.Q5ZAW1; -.
DR PaxDb; 39947-Q5ZAW1; -.
DR EnsemblPlants; Os01t0788400-01; Os01t0788400-01; Os01g0788400.
DR GeneID; 4325861; -.
DR Gramene; Os01t0788400-01; Os01t0788400-01; Os01g0788400.
DR KEGG; osa:4325861; -.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR HOGENOM; CLU_012243_9_2_1; -.
DR OMA; SIWAINV; -.
DR OrthoDB; 668039at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd15799; PMEI-like_4; 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 InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR NCBIfam; TIGR01614; PME_inhib; 1.
DR PANTHER; PTHR31707; PECTINESTERASE; 1.
DR PANTHER; PTHR31707:SF221; PECTINESTERASE_PECTINESTERASE INHIBITOR 18-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF04043; PMEI; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF101148; Plant invertase/pectin methylesterase inhibitor; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 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};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512, ECO:0000256|RuleBase:RU000589};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU000589};
KW Hydrolase {ECO:0000256|RuleBase:RU000589};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|ProteomicsDB:Q5ZAW1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059680};
KW Secreted {ECO:0000256|RuleBase:RU000589};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..193
FT /note="Pectinesterase inhibitor"
FT /evidence="ECO:0000259|SMART:SM00856"
FT ACT_SITE 383
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 546 AA; 58387 MW; 99319385F325E46F CRC64;
MRQRDEPLLS SPSHRNAYPC KLLSFTLLSL ATVLCLCAGA AFLLLSPTAT NLCASSPDPA
SCQAIVADAV LASPHSHPSR PAHVLRAILA TSLDRHDAAA EAVAGMRRRA SDPRHRAALE
DCVQLMGLAR DRLADAAGAP DVDVDVDDAR TWLSAVLTDH VTCLDGLDDG PLRDSVGAHL
EPLKSLASAS LAVLSAAGRG ARDVLAEAVD RFPSWLTARD RTLLDAGAGA VQADVVVAKD
GSGKYTTIKE AVDAAPDGGK SRYVIYVKKG VYKENLEVGK TKRVLMIVGD GMDQTVITGS
RNVVDGSTTF NSATLALSGD GIILQDLKVE NTAGAEKQQA VALRVSADRA VINRCRLDGY
QDTLYAHQLR QFYRDCAVSG TVDFVFGNAA AVLQGCVLTA RRPAQAQKNA VTAQGRTDPN
QNTGTSIHRC RVVPAPDLAP AAKQFPTFLG RPWKEYSRTV YMLSYLDSHV DPRGWLEWNG
ADFALKTLFY GEYQNQGPGA STAGRVNWPG YHVITDQSVA MQFTVGQFIQ GGNWLKATGV
NYNEGL
//
