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Protochlorophyllide reductase C, chloroplastic (PCR C) (EC 1.3.1.33) (NADPH-protochlorophyllide oxidoreductase C) (POR C)

 PORC_ARATH              Reviewed;         401 AA.
O48741;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
16-JAN-2019, entry version 155.
RecName: Full=Protochlorophyllide reductase C, chloroplastic;
Short=PCR C;
EC=1.3.1.33;
AltName: Full=NADPH-protochlorophyllide oxidoreductase C;
Short=POR C;
Flags: Precursor;
Name=PORC; OrderedLocusNames=At1g03630;
ORFNames=F21B7.24, F21B7.35, F21B7_11;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY LIGHT, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=10838072; DOI=10.1016/S0014-5793(00)01568-4;
Oosawa N., Masuda T., Awai K., Fusada N., Shimada H., Ohta H.,
Takamiya K.;
"Identification and light-induced expression of a novel gene of NADPH-
protochlorophyllide oxidoreductase isoform in Arabidopsis thaliana.";
FEBS Lett. 474:133-136(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
CHARACTERIZATION.
Su Q., Armstrong G., Frick G., Apel K.;
"The identification and characterization of a novel NADPH-
protochlorophyllide oxidoreductase C.";
(In) Proceedings of ELSO 2000: European Life Scientist Organization,
pp.72-72, Geneva (2000).
[7]
FUNCTION, AND INDUCTION BY LIGHT.
STRAIN=cv. Columbia;
PubMed=11785941; DOI=10.1023/A:1013699721301;
Su Q., Frick G., Armstrong G., Apel K.;
"POR C of Arabidopsis thaliana: a third light- and NADPH-dependent
protochlorophyllide oxidoreductase that is differentially regulated by
light.";
Plant Mol. Biol. 47:805-813(2001).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12848821; DOI=10.1046/j.1365-313X.2003.01798.x;
Frick G., Su Q., Apel K., Armstrong G.A.;
"An Arabidopsis porB porC double mutant lacking light-dependent
NADPH:protochlorophyllide oxidoreductases B and C is highly
chlorophyll-deficient and developmentally arrested.";
Plant J. 35:141-153(2003).
[9]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE FLU-CONTAINING
CHLOROPLAST MEMBRANE COMPLEX.
PubMed=22212719; DOI=10.1016/j.febslet.2011.12.029;
Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.;
"FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is
physically linked to the final steps of the Mg(++)-branch of this
pathway.";
FEBS Lett. 586:211-216(2012).
-!- FUNCTION: Phototransformation of protochlorophyllide (Pchlide) to
chlorophyllide (Chlide). {ECO:0000269|PubMed:11785941,
ECO:0000269|PubMed:12848821}.
-!- CATALYTIC ACTIVITY:
Reaction=chlorophyllide a + NADP(+) = H(+) + NADPH +
protochlorophyllide a; Xref=Rhea:RHEA:11132, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83348,
ChEBI:CHEBI:83350; EC=1.3.1.33;
-!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
biosynthesis.
-!- SUBUNIT: Part of the FLU-containing chloroplast membrane complex
composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1.
{ECO:0000269|PubMed:22212719}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
{ECO:0000269|PubMed:22212719}. Note=Prolamellar body of etiolated
seedling.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=O48741-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in flowers, upper leaves, rosette
and cauline leaves, stem. Not detectable in non-photosynthetic
tissues such as roots and seeds. {ECO:0000269|PubMed:10838072}.
-!- INDUCTION: Up-regulated by light. Not under circadian regulation.
{ECO:0000269|PubMed:10838072, ECO:0000269|PubMed:11785941}.
-!- DISRUPTION PHENOTYPE: No visible phenotype at the levels of the
whole plant or chloroplast ultrastructure; due to the redundancy
with PORB. Porb and porc double mutants have a seedling-lethal
pale-yellow xantha phenotype at the cotyledon stage, contain only
small amounts of Chla, and possess chloroplasts with mostly
unstacked thylakoid membranes. {ECO:0000269|PubMed:12848821}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. POR subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB035746; BAA96654.1; -; mRNA.
EMBL; AC002560; AAF86518.1; -; Genomic_DNA.
EMBL; CP002684; AEE27591.1; -; Genomic_DNA.
EMBL; AY048263; AAK82525.1; -; mRNA.
EMBL; AY133569; AAM91399.1; -; mRNA.
EMBL; AY088529; AAM66062.1; -; mRNA.
PIR; T00897; T00897.
RefSeq; NP_171860.1; NM_100243.4. [O48741-1]
UniGene; At.24740; -.
ProteinModelPortal; O48741; -.
SMR; O48741; -.
BioGrid; 24247; 12.
IntAct; O48741; 13.
MINT; O48741; -.
STRING; 3702.AT1G03630.1; -.
PaxDb; O48741; -.
PRIDE; O48741; -.
EnsemblPlants; AT1G03630.1; AT1G03630.1; AT1G03630. [O48741-1]
GeneID; 839009; -.
Gramene; AT1G03630.1; AT1G03630.1; AT1G03630. [O48741-1]
KEGG; ath:AT1G03630; -.
Araport; AT1G03630; -.
TAIR; locus:2020738; AT1G03630.
eggNOG; KOG1208; Eukaryota.
eggNOG; COG1028; LUCA.
InParanoid; O48741; -.
KO; K00218; -.
OrthoDB; 1032903at2759; -.
PhylomeDB; O48741; -.
BioCyc; ARA:AT1G03630-MONOMER; -.
BioCyc; MetaCyc:AT1G03630-MONOMER; -.
BRENDA; 1.3.1.33; 399.
UniPathway; UPA00668; -.
PRO; PR:O48741; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; O48741; baseline and differential.
Genevisible; O48741; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:TAIR.
GO; GO:0016630; F:protochlorophyllide reductase activity; IEA:UniProtKB-EC.
GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR005979; Prochl_reduct.
InterPro; IPR002347; SDR_fam.
PANTHER; PTHR44419; PTHR44419; 1.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01289; LPOR; 1.
1: Evidence at protein level;
Alternative splicing; Chlorophyll biosynthesis; Chloroplast;
Complete proteome; Membrane; NADP; Oxidoreductase; Photosynthesis;
Plastid; Reference proteome; Transit peptide.
TRANSIT 1 67 Chloroplast. {ECO:0000255}.
CHAIN 68 401 Protochlorophyllide reductase C,
chloroplastic.
/FTId=PRO_0000023289.
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


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