PORC_ARATH
ID PORC_ARATH Reviewed; 401 AA.
AC O48741;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protochlorophyllide reductase C, chloroplastic;
DE Short=PCR C;
DE EC=1.3.1.33;
DE AltName: Full=NADPH-protochlorophyllide oxidoreductase C;
DE Short=POR C;
DE Flags: Precursor;
GN Name=PORC; OrderedLocusNames=At1g03630;
GN ORFNames=F21B7.24, F21B7.35, F21B7_11;
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], INDUCTION BY LIGHT, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10838072; DOI=10.1016/s0014-5793(00)01568-4;
RA Oosawa N., Masuda T., Awai K., Fusada N., Shimada H., Ohta H., Takamiya K.;
RT "Identification and light-induced expression of a novel gene of NADPH-
RT protochlorophyllide oxidoreductase isoform in Arabidopsis thaliana.";
RL FEBS Lett. 474:133-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CHARACTERIZATION.
RA Su Q., Armstrong G., Frick G., Apel K.;
RT "The identification and characterization of a novel NADPH-
RT protochlorophyllide oxidoreductase C.";
RL (In) Proceedings of ELSO 2000: European Life Scientist Organization,
RL pp.72-72, Geneva (2000).
RN [7]
RP FUNCTION, AND INDUCTION BY LIGHT.
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12848821; DOI=10.1046/j.1365-313x.2003.01798.x;
RA Frick G., Su Q., Apel K., Armstrong G.A.;
RT "An Arabidopsis porB porC double mutant lacking light-dependent
RT NADPH:protochlorophyllide oxidoreductases B and C is highly chlorophyll-
RT deficient and developmentally arrested.";
RL Plant J. 35:141-153(2003).
RN [9]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST
RP MEMBRANE COMPLEX.
RX PubMed=22212719; DOI=10.1016/j.febslet.2011.12.029;
RA Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.;
RT "FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is
RT physically linked to the final steps of the Mg(++)-branch of this
RT pathway.";
RL FEBS Lett. 586:211-216(2012).
CC -!- FUNCTION: Phototransformation of protochlorophyllide (Pchlide) to
CC chlorophyllide (Chlide). {ECO:0000269|PubMed:11785941,
CC ECO:0000269|PubMed:12848821}.
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 -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: Part of the FLU-containing chloroplast membrane complex
CC composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1.
CC {ECO:0000269|PubMed:22212719}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:22212719}. Note=Prolamellar body of etiolated
CC seedling.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O48741-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, upper leaves, rosette and
CC cauline leaves, stem. Not detectable in non-photosynthetic tissues such
CC as roots and seeds. {ECO:0000269|PubMed:10838072}.
CC -!- INDUCTION: Up-regulated by light. Not under circadian regulation.
CC {ECO:0000269|PubMed:10838072, ECO:0000269|PubMed:11785941}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype at the levels of the whole
CC plant or chloroplast ultrastructure; due to the redundancy with PORB.
CC Porb and porc double mutants have a seedling-lethal pale-yellow xantha
CC phenotype at the cotyledon stage, contain only small amounts of Chla,
CC and possess chloroplasts with mostly unstacked thylakoid membranes.
CC {ECO:0000269|PubMed:12848821}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. POR subfamily. {ECO:0000305}.
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DR EMBL; AB035746; BAA96654.1; -; mRNA.
DR EMBL; AC002560; AAF86518.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27591.1; -; Genomic_DNA.
DR EMBL; AY048263; AAK82525.1; -; mRNA.
DR EMBL; AY133569; AAM91399.1; -; mRNA.
DR EMBL; AY088529; AAM66062.1; -; mRNA.
DR PIR; T00897; T00897.
DR RefSeq; NP_171860.1; NM_100243.4. [O48741-1]
DR AlphaFoldDB; O48741; -.
DR SMR; O48741; -.
DR BioGRID; 24247; 12.
DR IntAct; O48741; 13.
DR MINT; O48741; -.
DR STRING; 3702.AT1G03630.1; -.
DR MetOSite; O48741; -.
DR PaxDb; O48741; -.
DR PRIDE; O48741; -.
DR EnsemblPlants; AT1G03630.1; AT1G03630.1; AT1G03630. [O48741-1]
DR GeneID; 839009; -.
DR Gramene; AT1G03630.1; AT1G03630.1; AT1G03630. [O48741-1]
DR KEGG; ath:AT1G03630; -.
DR Araport; AT1G03630; -.
DR TAIR; locus:2020738; AT1G03630.
DR eggNOG; KOG1208; Eukaryota.
DR InParanoid; O48741; -.
DR PhylomeDB; O48741; -.
DR BioCyc; ARA:AT1G03630-MON; -.
DR BioCyc; MetaCyc:AT1G03630-MON; -.
DR BRENDA; 1.3.1.33; 399.
DR UniPathway; UPA00668; -.
DR PRO; PR:O48741; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48741; baseline and differential.
DR Genevisible; O48741; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:TAIR.
DR GO; GO:0016630; F:protochlorophyllide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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; Membrane;
KW NADP; Oxidoreductase; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..401
FT /note="Protochlorophyllide reductase C, chloroplastic"
FT /id="PRO_0000023289"
FT REGION 65..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43883 MW; 6F395276DCE54A3A CRC64;
MALQAAYSLL PSTISIQKEG KFNASLKETT FTGSSFSNHL RAEKISTLLT IKEQRRQKPR
FSTGIRAQTV TATPPANEAS PEQKKTERKG TAVITGASSG LGLATAKALA DTGKWHVIMA
CRNFLKAEKA ARSVGMSKED YTVMHLDLAS LESVKQFVEN FRRTEQPLDV LVCNAAVYQP
TAKEPSFTAE GFEISVGTNH LGHFLLSRLL LDDLKKSDYP SKRMIIVGSI TGNTNTLAGN
VPPKANLGDL RGLASGLNGQ NSSMIDGGEF DGAKAYKDSK VCNMLTMQEL HRRYHEETGV
TFASLYPGCI ATTGLFREHI PLFRLLFPPF QKYITKGYVS EEEAGKRLAQ VVSDPSLGKS
GVYWSWNNNS SSFENQLSKE ASDAEKAKKL WEVSEKLVGL A
