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PAO_ORYSJ
ID   PAO_ORYSJ               Reviewed;         529 AA.
AC   Q0DV66; Q10RT5;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Pheophorbide a oxygenase, chloroplastic {ECO:0000303|PubMed:21807436};
DE            Short=OsPaO {ECO:0000303|PubMed:21807436};
DE            Short=Pheide a oxygenase {ECO:0000305};
DE            EC=1.14.15.17 {ECO:0000250|UniProtKB:Q9FYC2};
DE   Flags: Precursor;
GN   Name=PAO {ECO:0000303|PubMed:21807436};
GN   OrderedLocusNames=Os03g0146400 {ECO:0000312|EMBL:BAS82280.1},
GN   LOC_Os03g05310 {ECO:0000312|EMBL:ABF93963.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
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   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=21807436; DOI=10.1016/j.jplph.2011.05.026;
RA   Tang Y., Li M., Chen Y., Wu P., Wu G., Jiang H.;
RT   "Knockdown of OsPAO and OsRCCR1 cause different plant death phenotypes in
RT   rice.";
RL   J. Plant Physiol. 168:1952-1959(2011).
CC   -!- FUNCTION: Catalyzes the key reaction of chlorophyll catabolism,
CC       porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a primary
CC       fluorescent catabolite (pFCC). Works in a two-step reaction with red
CC       chlorophyll catabolite reductase (RCCR). Creates the intermediate RCC
CC       through the opening of the porphyrin macrocycle by the introduction of
CC       one atom of molecular oxygen at the alpha-methine bridge. Seems to be
CC       specific for pheide a. Belongs to the chlorophyll catabolic enzymes
CC       (CCEs) (By similarity). May play a role in senescence and response to
CC       wounding (PubMed:21807436). {ECO:0000250|UniProtKB:Q9FYC2,
CC       ECO:0000269|PubMed:21807436}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + O2 + pheophorbide a + 2 reduced [2Fe-2S]-[ferredoxin]
CC         = 2 oxidized [2Fe-2S]-[ferredoxin] + red chlorophyll catabolite;
CC         Xref=Rhea:RHEA:48140, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:58687, ChEBI:CHEBI:58716;
CC         EC=1.14.15.17; Evidence={ECO:0000250|UniProtKB:Q9FYC2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48141;
CC         Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       degradation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves (PubMed:21807436). Expressed at
CC       low levels in roots, stems, panicles and seeds (PubMed:21807436).
CC       {ECO:0000269|PubMed:21807436}.
CC   -!- INDUCTION: Induced by wounding and senescence in leaves.
CC       {ECO:0000269|PubMed:21807436}.
CC   -!- MISCELLANEOUS: Plants silencing PAO die shortly after regeneration.
CC       {ECO:0000269|PubMed:21807436}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF93963.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DP000009; ABF93963.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014959; BAS82280.1; -; Genomic_DNA.
DR   RefSeq; XP_015633218.1; XM_015777732.1.
DR   AlphaFoldDB; Q0DV66; -.
DR   SMR; Q0DV66; -.
DR   STRING; 4530.OS03T0146400-01; -.
DR   PaxDb; Q0DV66; -.
DR   PRIDE; Q0DV66; -.
DR   EnsemblPlants; Os03t0146400-01; Os03t0146400-01; Os03g0146400.
DR   EnsemblPlants; Os03t0146400-02; Os03t0146400-02; Os03g0146400.
DR   GeneID; 4331611; -.
DR   Gramene; Os03t0146400-01; Os03t0146400-01; Os03g0146400.
DR   Gramene; Os03t0146400-02; Os03t0146400-02; Os03g0146400.
DR   KEGG; osa:4331611; -.
DR   eggNOG; ENOG502QQ8U; Eukaryota.
DR   HOGENOM; CLU_003927_1_0_1; -.
DR   InParanoid; Q0DV66; -.
DR   OMA; MWHDLTS; -.
DR   OrthoDB; 1199207at2759; -.
DR   BRENDA; 1.14.15.17; 8948.
DR   UniPathway; UPA00674; -.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010277; F:chlorophyllide a oxygenase [overall] activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0032441; F:pheophorbide a oxygenase activity; IBA:GO_Central.
DR   GO; GO:0008219; P:cell death; IEA:EnsemblPlants.
DR   GO; GO:0015996; P:chlorophyll catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR   GO; GO:0009908; P:flower development; IEA:EnsemblPlants.
DR   GO; GO:0010154; P:fruit development; IEA:EnsemblPlants.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR013626; PaO.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF08417; PaO; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Chlorophyll catabolism; Chloroplast; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..529
FT                   /note="Pheophorbide a oxygenase, chloroplastic"
FT                   /id="PRO_0000449574"
FT   DOMAIN          82..194
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         124
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         126
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         144
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         147
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   529 AA;  59074 MW;  E758572885CE9FE0 CRC64;
     MPVMAPTASL LLSPRPLPAS RRVPSLPALS ASGRLRLRRA RADTRLRVAA PPSVPGEADQ
     APGETEPSTS SADEKFVWRD HWYPVSLVED LDPSVPTPFQ LLNRDLVIWK DPKSGEWVAL
     DDRCPHRLAP LSEGRIDETG CLQCSYHGWS FDGSGACTRI PQAAPEGPEA KAVRSPKACA
     IKFPTLVSQG LLFVWPDENG WEKATATKPP MLPKEFEDPA FSTVTIQRDL YYGYDTLMEN
     VSDPSHIEFA HHKVTGRRDR ARPLPFKMES SGAWGYSGSN SGNPRISATF VAPCYALNKI
     EIDTKLPIFG DQKWVIWICS FNIPMAPGKT RSIVCSARNF FQFSMPGKAW WQLVPRWYEH
     WTSNLVYDGD MIVLQGQEKI FLSASKESSA DINQQYTKIT FTPTQADRFV LAFRAWLRKF
     GNSQPDWFGN PSQEVLPSTV LSKREMLDRY EQHTLKCSSC KGAYNAFQTL QKVFMGATVA
     FCATAGIPAD VQFRLLLAAA ALVSAAVAYA FYTLQKNFVF VDYVHAEID
 
 
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