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Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic (Mg-protoporphyrin IX monomethyl ester oxidative cyclase) (EC 1.14.13.81) (Copper response defect 1 protein) (Dicarboxylate diiron protein) (AtZIP) (MPE-cyclase)

 CRD1_ARATH              Reviewed;         409 AA.
Q9M591; O04051; Q38892; Q8GUS3; Q9M1K4;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
16-AUG-2005, sequence version 2.
25-APR-2018, entry version 124.
RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic;
Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase;
EC=1.14.13.81;
AltName: Full=Copper response defect 1 protein;
AltName: Full=Dicarboxylate diiron protein;
Short=AtZIP;
AltName: Full=MPE-cyclase;
Flags: Precursor;
Name=CRD1; Synonyms=ACSF, AT103, CHL27, ZIP;
OrderedLocusNames=At3g56940; ORFNames=F24I3.20;
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].
PubMed=9449833; DOI=10.1104/pp.116.1.27;
Zheng C.C., Porat R., Lu P., O'Neill S.D.;
"PNZIP is a novel mesophyll-specific cDNA that is regulated by
phytochrome and the circadian rhythm and encodes a protein with a
leucine zipper motif.";
Plant Physiol. 116:27-35(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10811605; DOI=10.1093/emboj/19.10.2139;
Moseley J.L., Quinn J., Eriksson M., Merchant S.;
"The Crd1 gene encodes a putative di-iron enzyme required for
photosystem I accumulation in copper deficiency and hypoxia in
Chlamydomonas reinhardtii.";
EMBO J. 19:2139-2151(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-76.
Liu N., Zheng C.;
"Cloning and characteristics of AT103 gene promoter.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 215-313.
STRAIN=cv. Columbia;
PubMed=9339905;
Pih K.T., Jang H.J., Kang S.G., Piao H.L., Hwang I.;
"Isolation of molecular markers for salt stress responses in
Arabidopsis thaliana.";
Mol. Cells 7:567-571(1997).
[7]
FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=14673103; DOI=10.1073/pnas.2136793100;
Tottey S., Block M.A., Allen M., Westergren T., Albrieux C.,
Scheller H.V., Merchant S., Jensen P.E.;
"Arabidopsis CHL27, located in both envelope and thylakoid membranes,
is required for the synthesis of protochlorophyllide.";
Proc. Natl. Acad. Sci. U.S.A. 100:16119-16124(2003).
[8]
FUNCTION.
PubMed=18682427; DOI=10.1093/pcp/pcn111;
Bang W.Y., Jeong I.S., Kim D.W., Im C.H., Ji C., Hwang S.M., Kim S.W.,
Son Y.S., Jeong J., Shiina T., Bahk J.D.;
"Role of Arabidopsis CHL27 protein for photosynthesis, chloroplast
development and gene expression profiling.";
Plant Cell Physiol. 49:1350-1363(2008).
[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: Catalyzes the formation of the isocyclic ring in
chlorophyll biosynthesis. Mediates the cyclase reaction, which
results in the formation of divinylprotochlorophyllide (Pchlide)
characteristic of all chlorophylls from magnesium-protoporphyrin
IX 13-monomethyl ester (MgPMME). {ECO:0000269|PubMed:14673103,
ECO:0000269|PubMed:18682427}.
-!- CATALYTIC ACTIVITY: Magnesium-protoporphyrin IX 13-monomethyl
ester + 3 NADPH + 3 O(2) = 3,8-divinyl protochlorophyllide + 3
NADP(+) + 5 H(2)O. {ECO:0000269|PubMed:14673103}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
-!- 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}.
-!- INTERACTION:
Q940U6:FLU; NbExp=5; IntAct=EBI-7632098, EBI-2319882;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane;
Peripheral membrane protein. Plastid, chloroplast thylakoid
membrane; Peripheral membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9M591-1; Sequence=Displayed;
-!- MISCELLANEOUS: Knock-down mutant (chl27-t) grow slowly with a pale
green appearance. confers also severe defects in chloroplast
development, including the unstacking of thylakoid membranes
(PubMed:18682427). {ECO:0000305|PubMed:18682427}.
-!- SIMILARITY: Belongs to the AcsF family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB18942.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U38232; AAB18942.1; ALT_INIT; mRNA.
EMBL; AF236101; AAF63476.1; -; mRNA.
EMBL; AL138655; CAB72164.1; -; Genomic_DNA.
EMBL; CP002686; AEE79589.1; -; Genomic_DNA.
EMBL; AY170319; AAO11785.1; -; Genomic_DNA.
EMBL; U75599; AAB51703.1; -; mRNA.
PIR; T47754; T47754.
RefSeq; NP_191253.1; NM_115553.4. [Q9M591-1]
UniGene; At.48778; -.
UniGene; At.70999; -.
ProteinModelPortal; Q9M591; -.
BioGrid; 10177; 1.
IntAct; Q9M591; 2.
MINT; Q9M591; -.
STRING; 3702.AT3G56940.1; -.
iPTMnet; Q9M591; -.
PaxDb; Q9M591; -.
PRIDE; Q9M591; -.
EnsemblPlants; AT3G56940.1; AT3G56940.1; AT3G56940. [Q9M591-1]
GeneID; 824861; -.
Gramene; AT3G56940.1; AT3G56940.1; AT3G56940. [Q9M591-1]
KEGG; ath:AT3G56940; -.
Araport; AT3G56940; -.
TAIR; locus:2080560; AT3G56940.
eggNOG; ENOG410IFW2; Eukaryota.
eggNOG; ENOG410XPVQ; LUCA.
HOGENOM; HOG000233491; -.
InParanoid; Q9M591; -.
KO; K04035; -.
OMA; NPLLAEC; -.
OrthoDB; EOG09360C27; -.
PhylomeDB; Q9M591; -.
BioCyc; ARA:AT3G56940-MONOMER; -.
BioCyc; MetaCyc:AT3G56940-MONOMER; -.
BRENDA; 1.14.13.81; 399.
UniPathway; UPA00668; -.
PRO; PR:Q9M591; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9M591; baseline and differential.
Genevisible; Q9M591; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
GO; GO:0003677; F:DNA binding; TAS:TAIR.
GO; GO:0048529; F:magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity; IMP:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
GO; GO:1901401; P:regulation of tetrapyrrole metabolic process; IMP:TAIR.
CDD; cd01047; ACSF; 1.
HAMAP; MF_01840; AcsF; 1.
InterPro; IPR008434; AcsF.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR003251; Rubrerythrin.
PANTHER; PTHR31053; PTHR31053; 1.
Pfam; PF02915; Rubrerythrin; 1.
SUPFAM; SSF47240; SSF47240; 1.
TIGRFAMs; TIGR02029; AcsF; 1.
1: Evidence at protein level;
Alternative splicing; Chlorophyll biosynthesis; Chloroplast;
Complete proteome; Iron; Membrane; Metal-binding; NADP;
Oxidoreductase; Photosynthesis; Plastid; Plastid inner membrane;
Reference proteome; Thylakoid; Transit peptide.
TRANSIT 1 36 Chloroplast. {ECO:0000255}.
CHAIN 37 409 Magnesium-protoporphyrin IX monomethyl
ester [oxidative] cyclase, chloroplastic.
/FTId=PRO_0000000598.
CONFLICT 14 14 F -> I (in Ref. 1; AAB18942).
{ECO:0000305}.
CONFLICT 157 157 L -> S (in Ref. 1; AAB18942).
{ECO:0000305}.
CONFLICT 216 219 TYLS -> RAAR (in Ref. 6; AAB51703).
{ECO:0000305}.
CONFLICT 299 299 C -> W (in Ref. 2; AAF63476).
{ECO:0000305}.
CONFLICT 310 312 LNT -> FKH (in Ref. 6; AAB51703).
{ECO:0000305}.
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


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