HCAR_ARATH
ID HCAR_ARATH Reviewed; 462 AA.
AC Q8GS60; O23023;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=7-hydroxymethyl chlorophyll a reductase, chloroplastic;
DE EC=1.17.7.2 {ECO:0000269|PubMed:21934147};
DE Flags: Precursor;
GN Name=HCAR; Synonyms=HMCR; OrderedLocusNames=At1g04620; ORFNames=T1G11.13;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=21934147; DOI=10.1105/tpc.111.089714;
RA Meguro M., Ito H., Takabayashi A., Tanaka R., Tanaka A.;
RT "Identification of the 7-hydroxymethyl chlorophyll a reductase of the
RT chlorophyll cycle in Arabidopsis.";
RL Plant Cell 23:3442-3453(2011).
RN [6]
RP INTERACTION WITH LHCII COMPLEX; SGR1; NYC1; NOL; PPH; PAO AND RCCR,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=23200839; DOI=10.1016/j.bbrc.2012.11.050;
RA Sakuraba Y., Kim Y.S., Yoo S.C., Hortensteiner S., Paek N.C.;
RT "7-Hydroxymethyl chlorophyll a reductase functions in metabolic channeling
RT of chlorophyll breakdown intermediates during leaf senescence.";
RL Biochem. Biophys. Res. Commun. 430:32-37(2013).
CC -!- FUNCTION: Probable iron-sulfur flavoprotein that converts 7-
CC hydroxymethyl chlorophyll a to chlorophyll a using ferredoxin as a
CC reducing equivalent. Catalyzes the reduction of a hydroxymethyl group
CC to a methyl group. Belongs to the chlorophyll catabolic enzymes (CCEs).
CC {ECO:0000269|PubMed:21934147}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorophyll a + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = 7(1)-
CC hydroxychlorophyll a + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:53544, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:58416, ChEBI:CHEBI:83377; EC=1.17.7.2;
CC Evidence={ECO:0000269|PubMed:21934147};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:21934147};
CC -!- COFACTOR:
CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC Evidence={ECO:0000269|PubMed:21934147};
CC -!- SUBUNIT: Interacts with SGR1, the chlorophyll catabolic enzymes (CCEs)
CC NYC1, NOL and RCCR, and the LHCII complex. Part of a SGR1-CCE-LHCII
CC complex, which acts in chlorophyll breakdown.
CC {ECO:0000269|PubMed:23200839}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21934147, ECO:0000269|PubMed:23200839}.
CC -!- DEVELOPMENTAL STAGE: Constantly expressed throughout development.
CC {ECO:0000269|PubMed:23200839}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but plants accumulate 7-hydroxymethyl chlorophyll a in
CC green leaves. {ECO:0000269|PubMed:21934147}.
CC -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002376; AAB80625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27722.1; -; Genomic_DNA.
DR EMBL; AK117982; BAC42618.1; -; mRNA.
DR EMBL; BT002029; AAN72040.1; -; mRNA.
DR EMBL; BT006603; AAP31947.1; -; mRNA.
DR PIR; H86178; H86178.
DR RefSeq; NP_171956.2; NM_100341.4.
DR PDB; 5DQR; X-ray; 2.70 A; A/B/C/D/E/F=26-462.
DR PDBsum; 5DQR; -.
DR AlphaFoldDB; Q8GS60; -.
DR SMR; Q8GS60; -.
DR BioGRID; 24707; 8.
DR IntAct; Q8GS60; 1.
DR MINT; Q8GS60; -.
DR STRING; 3702.AT1G04620.1; -.
DR PaxDb; Q8GS60; -.
DR PRIDE; Q8GS60; -.
DR ProteomicsDB; 247165; -.
DR EnsemblPlants; AT1G04620.1; AT1G04620.1; AT1G04620.
DR GeneID; 839472; -.
DR Gramene; AT1G04620.1; AT1G04620.1; AT1G04620.
DR KEGG; ath:AT1G04620; -.
DR Araport; AT1G04620; -.
DR TAIR; locus:2197848; AT1G04620.
DR eggNOG; ENOG502QR65; Eukaryota.
DR HOGENOM; CLU_038110_0_0_1; -.
DR InParanoid; Q8GS60; -.
DR OMA; WTGIVST; -.
DR OrthoDB; 788166at2759; -.
DR PhylomeDB; Q8GS60; -.
DR BioCyc; ARA:AT1G04620-MON; -.
DR BioCyc; MetaCyc:AT1G04620-MON; -.
DR BRENDA; 1.17.7.2; 399.
DR PRO; PR:Q8GS60; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GS60; baseline and differential.
DR Genevisible; Q8GS60; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0090415; F:7-hydroxymethyl chlorophyll a reductase activity; IDA:TAIR.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052592; F:oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor; IBA:GO_Central.
DR GO; GO:0033354; P:chlorophyll cycle; IDA:TAIR.
DR GO; GO:0015994; P:chlorophyll metabolic process; IDA:TAIR.
DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N.
DR InterPro; IPR045220; FRHB/FDHB/HCAR-like.
DR InterPro; IPR007525; FrhB_FdhB_C.
DR PANTHER; PTHR31332; PTHR31332; 1.
DR Pfam; PF04432; FrhB_FdhB_C; 1.
DR Pfam; PF04422; FrhB_FdhB_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..20
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 21..462
FT /note="7-hydroxymethyl chlorophyll a reductase,
FT chloroplastic"
FT /id="PRO_0000415615"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 161..170
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:5DQR"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5DQR"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:5DQR"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 364..375
FT /evidence="ECO:0007829|PDB:5DQR"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 407..428
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 430..437
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 440..448
FT /evidence="ECO:0007829|PDB:5DQR"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:5DQR"
SQ SEQUENCE 462 AA; 51661 MW; 71DB353FB5DB1AA5 CRC64;
MITVVTSRLS LLPPVFSVVN SSSSRSKDMN LEPKKKVKLR EDWREKSRPI PPGGTYPAKD
HCSQCGLCDT YYIAHVKEAC AFLGDGMSRI ESLEPVVHGR GRKADSLQDT YFGVHQEQLY
ARKLKPVEGA QWTGIVTTIA IEMLKSNMVE AVVCVQSDPE DRLSPRPVLA RTPEEVLAAR
GVKPTLSPNL NTLELIEASG VKRLLFCGVG CQVQALRSVE QHLNLEKLYV LGTNCVDNGT
RDGLDKFLKA ASKEPETVLH YEFMQDYKVQ LKHLDGHIEE VPYFSLPAND LVDVIAPSCY
SCFDYTNALA DLVIGYMGVP KYSGLNMTDH PQYITVRNER GKEMLSLVEN LLEITPTISS
GDRRPFVTET VKADDAAKFG QGPAQPAPLF VGNIIAFILN LVGPKGLEFA RYSLDYHTIR
NYLYVNRKWG KQRANTHMPS YAKKIVEMYN KNGQIDKMLS KK
