CRD1_ARATH
ID CRD1_ARATH Reviewed; 409 AA.
AC Q9M591; O04051; Q38892; Q8GUS3; Q9M1K4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic;
DE Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase;
DE EC=1.14.13.81;
DE AltName: Full=Copper response defect 1 protein;
DE AltName: Full=Dicarboxylate diiron protein;
DE Short=AtZIP;
DE AltName: Full=MPE-cyclase;
DE Flags: Precursor;
GN Name=CRD1; Synonyms=ACSF, AT103, CHL27, ZIP; OrderedLocusNames=At3g56940;
GN ORFNames=F24I3.20;
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].
RX PubMed=9449833; DOI=10.1104/pp.116.1.27;
RA Zheng C.C., Porat R., Lu P., O'Neill S.D.;
RT "PNZIP is a novel mesophyll-specific cDNA that is regulated by phytochrome
RT and the circadian rhythm and encodes a protein with a leucine zipper
RT motif.";
RL Plant Physiol. 116:27-35(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10811605; DOI=10.1093/emboj/19.10.2139;
RA Moseley J.L., Quinn J., Eriksson M., Merchant S.;
RT "The Crd1 gene encodes a putative di-iron enzyme required for photosystem I
RT accumulation in copper deficiency and hypoxia in Chlamydomonas
RT reinhardtii.";
RL EMBO J. 19:2139-2151(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-76.
RA Liu N., Zheng C.;
RT "Cloning and characteristics of AT103 gene promoter.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 215-313.
RC STRAIN=cv. Columbia;
RX PubMed=9339905;
RA Pih K.T., Jang H.J., Kang S.G., Piao H.L., Hwang I.;
RT "Isolation of molecular markers for salt stress responses in Arabidopsis
RT thaliana.";
RL Mol. Cells 7:567-571(1997).
RN [7]
RP FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=14673103; DOI=10.1073/pnas.2136793100;
RA Tottey S., Block M.A., Allen M., Westergren T., Albrieux C., Scheller H.V.,
RA Merchant S., Jensen P.E.;
RT "Arabidopsis CHL27, located in both envelope and thylakoid membranes, is
RT required for the synthesis of protochlorophyllide.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:16119-16124(2003).
RN [8]
RP FUNCTION.
RX PubMed=18682427; DOI=10.1093/pcp/pcn111;
RA Bang W.Y., Jeong I.S., Kim D.W., Im C.H., Ji C., Hwang S.M., Kim S.W.,
RA Son Y.S., Jeong J., Shiina T., Bahk J.D.;
RT "Role of Arabidopsis CHL27 protein for photosynthesis, chloroplast
RT development and gene expression profiling.";
RL Plant Cell Physiol. 49:1350-1363(2008).
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: Catalyzes the formation of the isocyclic ring in chlorophyll
CC biosynthesis. Mediates the cyclase reaction, which results in the
CC formation of divinylprotochlorophyllide (Pchlide) characteristic of all
CC chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester
CC (MgPMME). {ECO:0000269|PubMed:14673103, ECO:0000269|PubMed:18682427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + Mg-protoporphyrin IX 13-monomethyl ester + 3 NADPH +
CC 3 O2 = 3,8-divinyl protochlorophyllide a + 5 H2O + 3 NADP(+);
CC Xref=Rhea:RHEA:33235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58632, ChEBI:CHEBI:60491; EC=1.14.13.81;
CC Evidence={ECO:0000269|PubMed:14673103};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
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 -!- INTERACTION:
CC Q9M591; Q940U6: FLU; NbExp=5; IntAct=EBI-7632098, EBI-2319882;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Peripheral
CC membrane protein. Plastid, chloroplast thylakoid membrane; Peripheral
CC membrane protein.
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=Q9M591-1; Sequence=Displayed;
CC -!- MISCELLANEOUS: Knock-down mutant (chl27-t) grow slowly with a pale
CC green appearance. confers also severe defects in chloroplast
CC development, including the unstacking of thylakoid membranes
CC (PubMed:18682427). {ECO:0000305|PubMed:18682427}.
CC -!- SIMILARITY: Belongs to the AcsF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18942.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U38232; AAB18942.1; ALT_INIT; mRNA.
DR EMBL; AF236101; AAF63476.1; -; mRNA.
DR EMBL; AL138655; CAB72164.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79589.1; -; Genomic_DNA.
DR EMBL; AY170319; AAO11785.1; -; Genomic_DNA.
DR EMBL; U75599; AAB51703.1; -; mRNA.
DR PIR; T47754; T47754.
DR RefSeq; NP_191253.1; NM_115553.4. [Q9M591-1]
DR AlphaFoldDB; Q9M591; -.
DR BioGRID; 10177; 1.
DR IntAct; Q9M591; 2.
DR MINT; Q9M591; -.
DR STRING; 3702.AT3G56940.1; -.
DR iPTMnet; Q9M591; -.
DR PaxDb; Q9M591; -.
DR PRIDE; Q9M591; -.
DR ProteomicsDB; 224494; -. [Q9M591-1]
DR EnsemblPlants; AT3G56940.1; AT3G56940.1; AT3G56940. [Q9M591-1]
DR GeneID; 824861; -.
DR Gramene; AT3G56940.1; AT3G56940.1; AT3G56940. [Q9M591-1]
DR KEGG; ath:AT3G56940; -.
DR Araport; AT3G56940; -.
DR TAIR; locus:2080560; AT3G56940.
DR eggNOG; ENOG502QRIH; Eukaryota.
DR InParanoid; Q9M591; -.
DR PhylomeDB; Q9M591; -.
DR BioCyc; ARA:AT3G56940-MON; -.
DR BioCyc; MetaCyc:AT3G56940-MON; -.
DR BRENDA; 1.14.13.81; 399.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q9M591; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M591; baseline and differential.
DR Genevisible; Q9M591; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; TAS:TAIR.
DR GO; GO:0048529; F:magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:1901401; P:regulation of tetrapyrrole metabolic process; IMP:TAIR.
DR CDD; cd01047; ACSF; 1.
DR HAMAP; MF_01840; AcsF; 1.
DR InterPro; IPR008434; AcsF.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR003251; Rubrerythrin.
DR PANTHER; PTHR31053; PTHR31053; 1.
DR Pfam; PF02915; Rubrerythrin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR02029; AcsF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chlorophyll biosynthesis; Chloroplast; Iron;
KW Membrane; Metal-binding; NADP; Oxidoreductase; Photosynthesis; Plastid;
KW Plastid inner membrane; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..409
FT /note="Magnesium-protoporphyrin IX monomethyl ester
FT [oxidative] cyclase, chloroplastic"
FT /id="PRO_0000000598"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 14
FT /note="F -> I (in Ref. 1; AAB18942)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="L -> S (in Ref. 1; AAB18942)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..219
FT /note="TYLS -> RAAR (in Ref. 6; AAB51703)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="C -> W (in Ref. 2; AAF63476)"
FT /evidence="ECO:0000305"
FT CONFLICT 310..312
FT /note="LNT -> FKH (in Ref. 6; AAB51703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 47631 MW; B8808079C07B8C68 CRC64;
MAAEMALVKP ISKFSSPKLS NPSKFLSGRR FSTVIRMSAS SSPPPPTTAT SKSKKGTKKE
IQESLLTPRF YTTDFEEMEQ LFNTEINKNL NEAEFEALLQ EFKTDYNQTH FVRNKEFKEA
ADKLQGPLRQ IFVEFLERSC TAEFSGFLLY KELGRRLKKT NPVVAEIFSL MSRDEARHAG
FLNKGLSDFN LALDLGFLTK ARKYTFFKPK FIFYATYLSE KIGYWRYITI YRHLKENPEF
QCYPIFKYFE NWCQDENRHG DFFSALMKAQ PQFLNDWQAK LWSRFFCLSV YVTMYLNDCQ
RTNFYEGIGL NTKEFDMHVI IETNRTTARI FPAVLDVENP EFKRKLDRMV VSYEKLLAIG
ETDDASFIKT LKRIPLVTSL ASEILAAYLM PPVESGSVDF AEFEPNLVY
