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   16-JUN-2009, entry version 55.
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   Flags: Precursor;
GN   Name=CRD1; Synonyms=AT103, CHL27, ZIP; OrderedLocusNames=At3g56940;
GN   ORFNames=F24I3.20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98111485; 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
RT   phytochrome and the circadian rhythm and encodes a protein with a
RT   leucine zipper motif.";
RL   Plant Physiol. 116:27-35(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20271854; 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
RT   photosystem I accumulation in copper deficiency and hypoxia in
RT   Chlamydomonas reinhardtii.";
RL   EMBO J. 19:2139-2151(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 215-313.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=97479824; 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
RT   Arabidopsis thaliana.";
RL   Mol. Cells 7:567-571(1997).
RN   [6]
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.,
RA   Scheller H.V., Merchant S., Jensen P.E.;
RT   "Arabidopsis CHL27, located in both envelope and thylakoid membranes,
RT   is required for the synthesis of protochlorophyllide.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:16119-16124(2003).
CC   -!- FUNCTION: Catalyzes the formation of the isocyclic ring in
CC       chlorophyll biosynthesis. Mediates the cyclase reaction, which
CC       results in the formation of divinylprotochlorophyllide (Pchlide)
CC       characteristic of all chlorophylls from magnesium-protoporphyrin
CC       IX 13-monomethyl ester (MgPMME).
CC   -!- CATALYTIC ACTIVITY: Magnesium-protoporphyrin IX 13-monomethyl
CC       ester + NADPH + O(2) = 13(1)-hydroxy-magnesium-protoporphyrin IX
CC       13-monomethyl ester + NADP(+) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 13(1)-hydroxy-magnesium-protoporphyrin IX 13-
CC       monomethyl ester + NADPH + O(2) = 13(1)-oxo-magnesium-
CC       protoporphyrin IX 13-monomethyl ester + NADP(+) + 2 H(2)O.
CC   -!- CATALYTIC ACTIVITY: 13(1)-oxo-magnesium-protoporphyrin IX 13-
CC       monomethyl ester + NADPH + O(2) = divinylprotochlorophyllide +
CC       NADP(+) + 2 H(2)O.
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane;
CC       Peripheral membrane protein. Plastid, chloroplast thylakoid
CC       membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the acsF family.
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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; AY170319; AAO11785.1; -; Genomic_DNA.
DR   EMBL; U75599; AAB51703.1; -; mRNA.
DR   IPI; IPI00517126; -.
DR   PIR; T47754; T47754.
DR   RefSeq; NP_191253.1; -.
DR   UniGene; At.48778; -.
DR   PRIDE; Q9M591; -.
DR   GeneID; 824861; -.
DR   GenomeReviews; BA000014_GR; AT3G56940.
DR   KEGG; ath:AT3G56940; -.
DR   NMPDR; fig|3702.1.peg.17023; -.
DR   TAIR; At3g56940; -.
DR   OMA; Q9M591; TAEFSGC.
DR   BioCyc; MetaCyc:AT3G56940-MON; -.
DR   BRENDA; 1.14.13.81; 302.
DR   GermOnline; AT3G56940; Arabidopsis thaliana.
DR   GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; TAS:TAIR.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048529; F:magnesium-protoporphyrin IX monomethyl este...; IMP:TAIR.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   InterPro; IPR008434; AcsF.
DR   InterPro; IPR003251; Rubrerythrin.
DR   Pfam; PF02915; Rubrerythrin; 1.
DR   TIGRFAMs; TIGR02029; AcsF; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; Complete proteome; Iron;
KW   Membrane; Metal-binding; NADP; Oxidoreductase; Photosynthesis;
KW   Plastid; Plastid inner membrane; Thylakoid; Transit peptide.
FT   TRANSIT       1     36       Chloroplast (Potential).
FT   CHAIN        37    409       Magnesium-protoporphyrin IX monomethyl
FT                                ester [oxidative] cyclase, chloroplastic.
FT                                /FTId=PRO_0000000598.
FT   CONFLICT     14     14       F -> I (in Ref. 1).
FT   CONFLICT    157    157       L -> S (in Ref. 1; AAB18942).
FT   CONFLICT    216    219       TYLS -> RAAR (in Ref. 5).
FT   CONFLICT    299    299       C -> W (in Ref. 2; AAF63476).
FT   CONFLICT    310    312       LNT -> FKH (in Ref. 5).
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
//