PFBS_ARATH
ID PFBS_ARATH Reviewed; 329 AA.
AC Q9SR43; Q8L8Q6; Q9SS72;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phytochromobilin:ferredoxin oxidoreductase, chloroplastic {ECO:0000305};
DE EC=1.3.7.4 {ECO:0000269|PubMed:11226195};
DE AltName: Full=PFB synthase {ECO:0000305};
DE AltName: Full=PPhiB synthase {ECO:0000305};
DE AltName: Full=Phytochromobilin synthase {ECO:0000303|PubMed:11226195};
DE Flags: Precursor;
GN Name=HY2 {ECO:0000303|PubMed:11226195};
GN OrderedLocusNames=At3g09150 {ECO:0000312|Araport:AT3G09150};
GN ORFNames=F3L24.1 {ECO:0000312|EMBL:AAF14017.1},
GN MZB10.18 {ECO:0000312|EMBL:AAD56331.1};
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), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11226195; DOI=10.2307/3871286;
RA Kohchi T., Mukougawa K., Frankenberg N., Masuda M., Yokota A.,
RA Lagarias J.C.;
RT "The Arabidopsis HY2 gene encodes phytochromobilin synthase, a ferredoxin-
RT dependent biliverdin reductase.";
RL Plant Cell 13:425-436(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (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).
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.
CC -!- FUNCTION: Catalyzes the two-electron reduction of biliverdin IX-alpha
CC to the tetrapyrrole chromophore phytochromobilin (PPhiB).
CC {ECO:0000269|PubMed:11226195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-phytochromobilin + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC biliverdin IXalpha + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:16377, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57439, ChEBI:CHEBI:57991; EC=1.3.7.4;
CC Evidence={ECO:0000269|PubMed:11226195};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16379;
CC Evidence={ECO:0000269|PubMed:11226195};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11226195}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SR43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SR43-2; Sequence=VSP_008970;
CC -!- DISRUPTION PHENOTYPE: Elongated hypocotyl phenotype due to defect in
CC the tetrapyrrole chromophore phytochromobilin biosynthesis.
CC {ECO:0000269|PubMed:11226195}.
CC -!- SIMILARITY: Belongs to the HY2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD56331.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM67180.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB045112; BAB33374.1; -; mRNA.
DR EMBL; AC009326; AAD56331.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011436; AAF14017.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74730.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74731.1; -; Genomic_DNA.
DR EMBL; AY099706; AAM20557.1; -; mRNA.
DR EMBL; AY128900; AAM91300.1; -; mRNA.
DR EMBL; AY088874; AAM67180.1; ALT_INIT; mRNA.
DR RefSeq; NP_566344.2; NM_111750.4. [Q9SR43-1]
DR RefSeq; NP_850996.1; NM_180665.1. [Q9SR43-2]
DR AlphaFoldDB; Q9SR43; -.
DR SMR; Q9SR43; -.
DR BioGRID; 5403; 3.
DR STRING; 3702.AT3G09150.2; -.
DR PaxDb; Q9SR43; -.
DR PRIDE; Q9SR43; -.
DR ProteomicsDB; 236313; -. [Q9SR43-1]
DR EnsemblPlants; AT3G09150.1; AT3G09150.1; AT3G09150. [Q9SR43-2]
DR EnsemblPlants; AT3G09150.2; AT3G09150.2; AT3G09150. [Q9SR43-1]
DR GeneID; 820069; -.
DR Gramene; AT3G09150.1; AT3G09150.1; AT3G09150. [Q9SR43-2]
DR Gramene; AT3G09150.2; AT3G09150.2; AT3G09150. [Q9SR43-1]
DR KEGG; ath:AT3G09150; -.
DR Araport; AT3G09150; -.
DR TAIR; locus:2083484; AT3G09150.
DR eggNOG; ENOG502QXET; Eukaryota.
DR InParanoid; Q9SR43; -.
DR OrthoDB; 1006467at2759; -.
DR PhylomeDB; Q9SR43; -.
DR BioCyc; ARA:AT3G09150-MON; -.
DR BioCyc; MetaCyc:AT3G09150-MON; -.
DR BRENDA; 1.3.7.4; 399.
DR PRO; PR:Q9SR43; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR43; baseline and differential.
DR Genevisible; Q9SR43; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0050619; F:phytochromobilin:ferredoxin oxidoreductase activity; IDA:TAIR.
DR GO; GO:0010019; P:chloroplast-nucleus signaling pathway; IMP:TAIR.
DR GO; GO:0010024; P:phytochromobilin biosynthetic process; IEA:InterPro.
DR InterPro; IPR009249; Ferredoxin-dep_bilin_Rdtase.
DR PANTHER; PTHR34557; PTHR34557; 1.
DR Pfam; PF05996; Fe_bilin_red; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..329
FT /note="Phytochromobilin:ferredoxin oxidoreductase,
FT chloroplastic"
FT /id="PRO_0000013609"
FT VAR_SEQ 75..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_008970"
FT CONFLICT 39
FT /note="K -> N (in Ref. 5; AAM67180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 38130 MW; 98727CD1778D973C CRC64;
MALSMEFGFS IGSCFKAPNP PVLISASPNK INFTLRRRKK RFLLRVSAVS YKEFAESALE
ETRKRIVLEP SHLQEKYSSM TGLDGKTELQ MLAFKSSKIR LLRSMAIENE TMQVFDFAGF
MEPEYDTPIF CANFFTSTNV NIVVLDLNPL HQLTDQTDYQ DKYYNKIMSI YHKYAETFPW
GGKLTGESIK FFSPLVMWTR FSSSKEKHKA LFSAFLEYYQ AWLEMTIQVR EEMEPSHVRA
NCEAQHKYLT WRAQKDPGHG LLKRLVGEAK AKELLRDFLF NGVDELGTKT FIDYFPEYQT
EDGTVSDKRS IIGKSYETRP WDLTGQFIG
