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Protein

7-hydroxymethyl chlorophyll a reductase, chloroplastic

Gene

HCAR

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable iron-sulfur flavoprotein that converts 7-hydroxymethyl chlorophyll a to chlorophyll a using ferredoxin as a reducing equivalent. Catalyzes the reduction of a hydroxymethyl group to a methyl group. Belongs to the chlorophyll catabolic enzymes (CCEs).1 Publication

Catalytic activityi

71-hydroxychlorophyllide a + 2 reduced ferredoxin + 2 H+ = chlorophyll a + 2 oxidized ferredoxin + H2O.1 Publication

Cofactori

Protein has several cofactor binding sites:

GO - Molecular functioni

GO - Biological processi

  • chlorophyll cycle Source: TAIR
  • chlorophyll metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT1G04620-MONOMER.
MetaCyc:AT1G04620-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
7-hydroxymethyl chlorophyll a reductase, chloroplastic (EC:1.17.7.2)
Gene namesi
Name:HCAR
Synonyms:HMCR
Ordered Locus Names:At1g04620
ORF Names:T1G11.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G04620.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but plants accumulate 7-hydroxymethyl chlorophyll a in green leaves.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020ChloroplastSequence analysisAdd
BLAST
Chaini21 – 4624427-hydroxymethyl chlorophyll a reductase, chloroplasticPRO_0000415615Add
BLAST

Proteomic databases

PaxDbiQ8GS60.
PRIDEiQ8GS60.

Expressioni

Developmental stagei

Constantly expressed throughout development.1 Publication

Gene expression databases

GenevisibleiQ8GS60. AT.

Interactioni

Subunit structurei

Interacts with SGR1, the chlorophyll catabolic enzymes (CCEs) NYC1, NOL and RCCR, and the LHCII complex. Part of a SGR1-CCE-LHCII complex, which acts in chlorophyll breakdown.1 Publication

Protein-protein interaction databases

BioGridi24707. 8 interactions.
IntActiQ8GS60. 1 interaction.
STRINGi3702.AT1G04620.1.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 463Combined sources
Helixi59 – 613Combined sources
Helixi67 – 693Combined sources
Helixi71 – 788Combined sources
Helixi86 – 894Combined sources
Helixi90 – 978Combined sources
Helixi107 – 1126Combined sources
Beta strandi116 – 12510Combined sources
Beta strandi130 – 1334Combined sources
Helixi135 – 14511Combined sources
Beta strandi150 – 1589Combined sources
Beta strandi161 – 17010Combined sources
Helixi173 – 1775Combined sources
Helixi193 – 1975Combined sources
Turni198 – 2003Combined sources
Beta strandi203 – 2086Combined sources
Helixi210 – 2189Combined sources
Helixi220 – 2234Combined sources
Beta strandi226 – 2338Combined sources
Helixi241 – 25111Combined sources
Beta strandi257 – 2637Combined sources
Beta strandi267 – 2737Combined sources
Beta strandi278 – 2825Combined sources
Helixi283 – 2853Combined sources
Turni288 – 2903Combined sources
Helixi291 – 2933Combined sources
Helixi297 – 3004Combined sources
Beta strandi310 – 3167Combined sources
Helixi327 – 3293Combined sources
Beta strandi332 – 3365Combined sources
Helixi339 – 3468Combined sources
Helixi347 – 3515Combined sources
Beta strandi352 – 3565Combined sources
Beta strandi359 – 3613Combined sources
Helixi364 – 37512Combined sources
Turni378 – 3803Combined sources
Helixi389 – 40214Combined sources
Helixi407 – 42822Combined sources
Helixi430 – 4378Combined sources
Helixi440 – 4489Combined sources
Helixi454 – 4596Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5DQRX-ray2.70A/B/C/D/E/F26-462[»]
ProteinModelPortaliQ8GS60.
SMRiQ8GS60. Positions 130-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FrhB family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IGX7. Eukaryota.
COG1035. LUCA.
HOGENOMiHOG000148137.
InParanoidiQ8GS60.
KOiK18010.
OMAiYVLGTPC.
PhylomeDBiQ8GS60.

Family and domain databases

InterProiIPR007516. Co_F420_Hydgase/DH_bsu_N.
IPR007525. FrhB_FdhB_C.
[Graphical view]
PfamiPF04432. FrhB_FdhB_C. 1 hit.
PF04422. FrhB_FdhB_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8GS60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITVVTSRLS LLPPVFSVVN SSSSRSKDMN LEPKKKVKLR EDWREKSRPI
60 70 80 90 100
PPGGTYPAKD HCSQCGLCDT YYIAHVKEAC AFLGDGMSRI ESLEPVVHGR
110 120 130 140 150
GRKADSLQDT YFGVHQEQLY ARKLKPVEGA QWTGIVTTIA IEMLKSNMVE
160 170 180 190 200
AVVCVQSDPE DRLSPRPVLA RTPEEVLAAR GVKPTLSPNL NTLELIEASG
210 220 230 240 250
VKRLLFCGVG CQVQALRSVE QHLNLEKLYV LGTNCVDNGT RDGLDKFLKA
260 270 280 290 300
ASKEPETVLH YEFMQDYKVQ LKHLDGHIEE VPYFSLPAND LVDVIAPSCY
310 320 330 340 350
SCFDYTNALA DLVIGYMGVP KYSGLNMTDH PQYITVRNER GKEMLSLVEN
360 370 380 390 400
LLEITPTISS GDRRPFVTET VKADDAAKFG QGPAQPAPLF VGNIIAFILN
410 420 430 440 450
LVGPKGLEFA RYSLDYHTIR NYLYVNRKWG KQRANTHMPS YAKKIVEMYN
460
KNGQIDKMLS KK
Length:462
Mass (Da):51,661
Last modified:March 1, 2003 - v1
Checksum:i71DB353FB5DB1AA5
GO

Sequence cautioni

The sequence AAB80625.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002376 Genomic DNA. Translation: AAB80625.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE27722.1.
AK117982 mRNA. Translation: BAC42618.1.
BT002029 mRNA. Translation: AAN72040.1.
BT006603 mRNA. Translation: AAP31947.1.
PIRiH86178.
RefSeqiNP_171956.2. NM_100341.3.
UniGeneiAt.42441.

Genome annotation databases

EnsemblPlantsiAT1G04620.1; AT1G04620.1; AT1G04620.
GeneIDi839472.
GrameneiAT1G04620.1; AT1G04620.1; AT1G04620.
KEGGiath:AT1G04620.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002376 Genomic DNA. Translation: AAB80625.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE27722.1.
AK117982 mRNA. Translation: BAC42618.1.
BT002029 mRNA. Translation: AAN72040.1.
BT006603 mRNA. Translation: AAP31947.1.
PIRiH86178.
RefSeqiNP_171956.2. NM_100341.3.
UniGeneiAt.42441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5DQRX-ray2.70A/B/C/D/E/F26-462[»]
ProteinModelPortaliQ8GS60.
SMRiQ8GS60. Positions 130-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi24707. 8 interactions.
IntActiQ8GS60. 1 interaction.
STRINGi3702.AT1G04620.1.

Proteomic databases

PaxDbiQ8GS60.
PRIDEiQ8GS60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G04620.1; AT1G04620.1; AT1G04620.
GeneIDi839472.
GrameneiAT1G04620.1; AT1G04620.1; AT1G04620.
KEGGiath:AT1G04620.

Organism-specific databases

TAIRiAT1G04620.

Phylogenomic databases

eggNOGiENOG410IGX7. Eukaryota.
COG1035. LUCA.
HOGENOMiHOG000148137.
InParanoidiQ8GS60.
KOiK18010.
OMAiYVLGTPC.
PhylomeDBiQ8GS60.

Enzyme and pathway databases

BioCyciARA:AT1G04620-MONOMER.
MetaCyc:AT1G04620-MONOMER.

Miscellaneous databases

PROiQ8GS60.

Gene expression databases

GenevisibleiQ8GS60. AT.

Family and domain databases

InterProiIPR007516. Co_F420_Hydgase/DH_bsu_N.
IPR007525. FrhB_FdhB_C.
[Graphical view]
PfamiPF04432. FrhB_FdhB_C. 1 hit.
PF04422. FrhB_FdhB_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    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.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Identification of the 7-hydroxymethyl chlorophyll a reductase of the chlorophyll cycle in Arabidopsis."
    Meguro M., Ito H., Takabayashi A., Tanaka R., Tanaka A.
    Plant Cell 23:3442-3453(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  6. "7-Hydroxymethyl chlorophyll a reductase functions in metabolic channeling of chlorophyll breakdown intermediates during leaf senescence."
    Sakuraba Y., Kim Y.S., Yoo S.C., Hortensteiner S., Paek N.C.
    Biochem. Biophys. Res. Commun. 430:32-37(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LHCII COMPLEX; SGR1; NYC1; NOL; PPH; PAO AND RCCR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiHCAR_ARATH
AccessioniPrimary (citable) accession number: Q8GS60
Secondary accession number(s): O23023
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.