PORA_ARATH
ID PORA_ARATH Reviewed; 405 AA.
AC Q42536; B9DGY6; Q9FK22;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protochlorophyllide reductase A, chloroplastic;
DE Short=PCR A;
DE EC=1.3.1.33 {ECO:0000305|PubMed:22278767};
DE AltName: Full=NADPH-protochlorophyllide oxidoreductase A;
DE Short=POR A;
DE Flags: Precursor;
GN Name=PORA; OrderedLocusNames=At5g54190; ORFNames=K18G13.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7659751; DOI=10.1104/pp.108.4.1505;
RA Armstrong G.A., Runge S., Frick G., Sperling U., Apel K.;
RT "Identification of NADPH:protochlorophyllide oxidoreductases A and B: a
RT branched pathway for light-dependent chlorophyll biosynthesis in
RT Arabidopsis thaliana.";
RL Plant Physiol. 108:1505-1517(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, INDUCTION BY LIGHT, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=11785941; DOI=10.1023/a:1013699721301;
RA Su Q., Frick G., Armstrong G., Apel K.;
RT "POR C of Arabidopsis thaliana: a third light- and NADPH-dependent
RT protochlorophyllide oxidoreductase that is differentially regulated by
RT light.";
RL Plant Mol. Biol. 47:805-813(2001).
RN [7]
RP INTERACTION WITH OP161 AND TOC33.
RX PubMed=15773849; DOI=10.1111/j.1365-313x.2005.02353.x;
RA Reinbothe S., Pollmann S., Springer A., James R.J., Tichtinsky G.,
RA Reinbothe C.;
RT "A role of Toc33 in the protochlorophyllide-dependent plastid import
RT pathway of NADPH:protochlorophyllide oxidoreductase (POR) A.";
RL Plant J. 42:1-12(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15842619; DOI=10.1111/j.1365-313x.2005.02374.x;
RA Kim C., Ham H., Apel K.;
RT "Multiplicity of different cell- and organ-specific import routes for the
RT NADPH-protochlorophyllide oxidoreductases A and B in plastids of
RT Arabidopsis seedlings.";
RL Plant J. 42:329-340(2005).
RN [9]
RP FUNCTION.
RX PubMed=20012672; DOI=10.1007/s11103-009-9582-y;
RA Paddock T.N., Mason M.E., Lima D.F., Armstrong G.A.;
RT "Arabidopsis protochlorophyllide oxidoreductase A (PORA) restores bulk
RT chlorophyll synthesis and normal development to a porB porC double
RT mutant.";
RL Plant Mol. Biol. 72:445-457(2010).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22278767; DOI=10.1007/s11103-012-9873-6;
RA Paddock T., Lima D., Mason M.E., Apel K., Armstrong G.A.;
RT "Arabidopsis light-dependent protochlorophyllide oxidoreductase A (PORA) is
RT essential for normal plant growth and development.";
RL Plant Mol. Biol. 78:447-460(2012).
RN [11]
RP INTERACTION WITH CPP1.
RX PubMed=25901327; DOI=10.1073/pnas.1506339112;
RA Reinbothe S., Gray J., Rustgi S., von Wettstein D., Reinbothe C.;
RT "Cell growth defect factor 1 is crucial for the plastid import of
RT NADPH:protochlorophyllide oxidoreductase A in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5838-5843(2015).
CC -!- FUNCTION: Phototransformation of protochlorophyllide (Pchlide) to
CC chlorophyllide (Chlide). PORA may also function as a photoprotectant
CC during the transitory stage from dark to light. Functions in
CC skotomorphogenesis, photomorphogenesis and throughout the plant life
CC under specific light conditions. {ECO:0000269|PubMed:11785941,
CC ECO:0000269|PubMed:20012672, ECO:0000269|PubMed:22278767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorophyllide a + NADP(+) = H(+) + NADPH +
CC protochlorophyllide a; Xref=Rhea:RHEA:11132, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83348,
CC ChEBI:CHEBI:83350; EC=1.3.1.33;
CC Evidence={ECO:0000305|PubMed:22278767};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11134;
CC Evidence={ECO:0000305|PubMed:22278767};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: Forms large complexes including TOC33, pPORA and OEP161 during
CC pPORA import into plastids at the plastid envelope membrane. Interacts
CC with CPP1 during plastid import (PubMed:25901327).
CC {ECO:0000269|PubMed:25901327}.
CC -!- INTERACTION:
CC Q42536; Q8GXW1: RGL2; NbExp=5; IntAct=EBI-4424685, EBI-963665;
CC Q42536; Q93XX2: SEOA; NbExp=4; IntAct=EBI-4424685, EBI-4424691;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15842619}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q42536-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q42536-2; Sequence=VSP_046548;
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings. Not detected in
CC leaves. {ECO:0000269|PubMed:7659751}.
CC -!- DEVELOPMENTAL STAGE: Etiolated seedlings. {ECO:0000269|PubMed:11785941,
CC ECO:0000269|PubMed:7659751}.
CC -!- INDUCTION: Down-regulated by light. {ECO:0000269|PubMed:11785941}.
CC -!- DISRUPTION PHENOTYPE: Lethal under normal growth conditions and light-
CC green stunted plants when grown in presence of sucrose.
CC {ECO:0000269|PubMed:22278767}.
CC -!- MISCELLANEOUS: The presence of TOC33 is not required for the import of
CC PORA into plastids. {ECO:0000305|PubMed:15842619}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. POR subfamily. {ECO:0000305}.
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DR EMBL; U29699; AAC49043.1; -; mRNA.
DR EMBL; AB013387; BAB11581.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96464.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96465.1; -; Genomic_DNA.
DR EMBL; BT003853; AAO41903.1; -; mRNA.
DR EMBL; BT005080; AAO50613.1; -; mRNA.
DR EMBL; AK317329; BAH20003.1; -; mRNA.
DR RefSeq; NP_001032072.1; NM_001036995.1. [Q42536-2]
DR RefSeq; NP_200230.1; NM_124799.4. [Q42536-1]
DR AlphaFoldDB; Q42536; -.
DR SMR; Q42536; -.
DR BioGRID; 20751; 8.
DR IntAct; Q42536; 2.
DR STRING; 3702.AT5G54190.1; -.
DR PaxDb; Q42536; -.
DR PRIDE; Q42536; -.
DR ProteomicsDB; 249050; -. [Q42536-1]
DR EnsemblPlants; AT5G54190.1; AT5G54190.1; AT5G54190. [Q42536-1]
DR EnsemblPlants; AT5G54190.2; AT5G54190.2; AT5G54190. [Q42536-2]
DR GeneID; 835507; -.
DR Gramene; AT5G54190.1; AT5G54190.1; AT5G54190. [Q42536-1]
DR Gramene; AT5G54190.2; AT5G54190.2; AT5G54190. [Q42536-2]
DR KEGG; ath:AT5G54190; -.
DR Araport; AT5G54190; -.
DR TAIR; locus:2153438; AT5G54190.
DR eggNOG; KOG1208; Eukaryota.
DR InParanoid; Q42536; -.
DR PhylomeDB; Q42536; -.
DR BioCyc; ARA:AT5G54190-MON; -.
DR BRENDA; 1.3.1.33; 399.
DR BRENDA; 1.3.7.7; 399.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q42536; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42536; baseline and differential.
DR Genevisible; Q42536; AT.
DR GO; GO:0009507; C:chloroplast; NAS:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0016630; F:protochlorophyllide reductase activity; IMP:UniProtKB.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009640; P:photomorphogenesis; IMP:UniProtKB.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR GO; GO:0009647; P:skotomorphogenesis; IMP:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005979; Prochl_reduct.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR44419; PTHR44419; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01289; LPOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chlorophyll biosynthesis; Chloroplast; NADP;
KW Oxidoreductase; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..405
FT /note="Protochlorophyllide reductase A, chloroplastic"
FT /id="PRO_0000023287"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_046548"
FT CONFLICT 37
FT /note="V -> I (in Ref. 1; AAC49043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 43863 MW; EB82F2CEF0480D2E CRC64;
MALQAASLVS SAFSVRKDGK LNASASSSFK ESSLFGVSLS EQSKADFVSS SLRCKREQSL
RNNKAIIRAQ AIATSTPSVT KSSLDRKKTL RKGNVVVTGA SSGLGLATAK ALAETGKWHV
IMACRDFLKA ERAAQSAGMP KDSYTVMHLD LASLDSVRQF VDNFRRAEMP LDVLVCNAAV
YQPTANQPTF TAEGFELSVG INHLGHFLLS RLLIDDLKNS DYPSKRLIIV GSITGNTNTL
AGNVPPKANL GDLRGLAGGL NGLNSSAMID GGDFVGAKAY KDSKVCNMLT MQEFHRRFHE
DTGITFASLY PGCIATTGLF REHIPLFRTL FPPFQKYITK GYVSESEAGK RLAQVVADPS
LTKSGVYWSW NKTSASFENQ LSQEASDVEK ARRVWEVSEK LVGLA
