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Magnesium-chelatase subunit ChlD, chloroplastic (Mg-chelatase subunit D) (EC 6.6.1.1) (Mg-protoporphyrin IX chelatase subunit ChlD) (Protein ALBINA 1) (Protein PIGMENT DEFECTIVE EMBRYO 166)

 CHLD_ARATH              Reviewed;         760 AA.
Q9SJE1; B9DFK0; Q8GUL4; Q8VZU7; Q93YN7; Q9SWY5;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 3.
25-OCT-2017, entry version 131.
RecName: Full=Magnesium-chelatase subunit ChlD, chloroplastic;
Short=Mg-chelatase subunit D;
EC=6.6.1.1;
AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlD;
AltName: Full=Protein ALBINA 1;
AltName: Full=Protein PIGMENT DEFECTIVE EMBRYO 166;
Flags: Precursor;
Name=CHLD; Synonyms=ALB1, PDE166; OrderedLocusNames=At1g08520;
ORFNames=T27G7.20;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-441.
STRAIN=cv. Columbia; TISSUE=Rosette leaf;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-759.
STRAIN=cv. C24;
Green J., Jensen P.E., Gibson L.C.D., Hunter C.N.;
"Characterization of the magnesium protoporphyrin chelatase chlD
subunit from Arabidopsis thaliana cv. c24.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19812694; DOI=10.1371/journal.pone.0007386;
Meinke D., Sweeney C., Muralla R.;
"Integrating the genetic and physical maps of Arabidopsis thaliana:
identification of mapped alleles of cloned essential (EMB) genes.";
PLoS ONE 4:E7386-E7386(2009).
[8]
INTERACTION WITH CHLI1 AND CHLD, AND FUNCTION.
PubMed=23011401; DOI=10.1007/s11103-012-9965-3;
Du S.Y., Zhang X.F., Lu Z., Xin Q., Wu Z., Jiang T., Lu Y., Wang X.F.,
Zhang D.P.;
"Roles of the different components of magnesium chelatase in abscisic
acid signal transduction.";
Plant Mol. Biol. 80:519-537(2012).
[9]
INDUCTION BY LIGHT.
PubMed=18846290; DOI=10.1039/b802596g;
Stephenson P.G., Terry M.J.;
"Light signalling pathways regulating the Mg-chelatase branchpoint of
chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.";
Photochem. Photobiol. Sci. 7:1243-1252(2008).
-!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the
insertion of magnesium ion into protoporphyrin IX to yield Mg-
protoporphyrin IX. The magnesium-chelatase is a complex of three
subunits, CHLI, CHLD and CHLH. The reaction takes place in two
steps, with an ATP-dependent activation followed by an ATP-
dependent chelation step. Does not bind abscisic acid.
{ECO:0000269|PubMed:19812694, ECO:0000269|PubMed:23011401}.
-!- CATALYTIC ACTIVITY: ATP + protoporphyrin IX + Mg(2+) + H(2)O = ADP
+ phosphate + Mg-protoporphyrin IX + 2 H(+).
-!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
biosynthesis.
-!- SUBUNIT: The magnesium chelatase complex is a heterotrimer
consisting of subunits CHLI, CHLD, AND CHLH. Interacts with CHLI1
and CHLH. {ECO:0000269|PubMed:23011401}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
-!- INDUCTION: Not regulated by light. {ECO:0000269|PubMed:18846290}.
-!- DISRUPTION PHENOTYPE: Pigment defective seeds and embryos.
{ECO:0000269|PubMed:19812694}.
-!- MISCELLANEOUS: Over-expression of CHLD has no impact on abscisic
acid sensitivity. {ECO:0000305|PubMed:23011401}.
-!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF22895.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAO00766.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC006932; AAF22895.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE28301.1; -; Genomic_DNA.
EMBL; AY063821; AAL36177.1; -; mRNA.
EMBL; AY091402; AAM14341.1; -; mRNA.
EMBL; AK226535; BAE98674.1; -; mRNA.
EMBL; AK316801; BAH19517.1; -; mRNA.
EMBL; AF083555; AAD52031.1; -; mRNA.
EMBL; BT002406; AAO00766.1; ALT_INIT; mRNA.
EMBL; AY059906; AAL24388.1; -; mRNA.
EMBL; AY114693; AAM48012.1; -; mRNA.
PIR; B86218; B86218.
RefSeq; NP_563821.2; NM_100725.4.
UniGene; At.11572; -.
ProteinModelPortal; Q9SJE1; -.
SMR; Q9SJE1; -.
BioGrid; 22615; 1.
STRING; 3702.AT1G08520.1; -.
PaxDb; Q9SJE1; -.
PRIDE; Q9SJE1; -.
EnsemblPlants; AT1G08520.1; AT1G08520.1; AT1G08520.
GeneID; 837374; -.
Gramene; AT1G08520.1; AT1G08520.1; AT1G08520.
KEGG; ath:AT1G08520; -.
Araport; AT1G08520; -.
TAIR; locus:2201796; AT1G08520.
eggNOG; ENOG410IJDJ; Eukaryota.
eggNOG; COG1239; LUCA.
eggNOG; COG1240; LUCA.
HOGENOM; HOG000225092; -.
InParanoid; Q9SJE1; -.
KO; K03404; -.
OMA; MQSAKGA; -.
OrthoDB; EOG09360533; -.
PhylomeDB; Q9SJE1; -.
BioCyc; ARA:AT1G08520-MONOMER; -.
BioCyc; MetaCyc:AT1G08520-MONOMER; -.
UniPathway; UPA00668; -.
PRO; PR:Q9SJE1; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SJE1; baseline and differential.
Genevisible; Q9SJE1; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
GO; GO:0010007; C:magnesium chelatase complex; TAS:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
InterPro; IPR000523; Mg_chelatse_chII_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF01078; Mg_chelatase; 1.
Pfam; PF13519; VWA_2; 1.
SMART; SM00382; AAA; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53300; SSF53300; 2.
TIGRFAMs; TIGR02031; BchD-ChlD; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
ATP-binding; Chlorophyll biosynthesis; Chloroplast; Complete proteome;
Ligase; Nucleotide-binding; Photosynthesis; Plastid;
Reference proteome; Transit peptide.
TRANSIT 1 49 Chloroplast. {ECO:0000255}.
CHAIN 50 760 Magnesium-chelatase subunit ChlD,
chloroplastic.
/FTId=PRO_0000002798.
DOMAIN 558 754 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
COMPBIAS 404 418 Pro-rich.
COMPBIAS 422 456 Glu-rich.
CONFLICT 70 70 D -> E (in Ref. 6; AAD52031).
{ECO:0000305}.
CONFLICT 150 150 D -> N (in Ref. 6; AAD52031).
{ECO:0000305}.
CONFLICT 270 270 G -> S (in Ref. 6; AAD52031).
{ECO:0000305}.
CONFLICT 285 286 Missing (in Ref. 6; AAD52031).
{ECO:0000305}.
CONFLICT 314 314 R -> S (in Ref. 6; AAD52031).
{ECO:0000305}.
CONFLICT 379 379 E -> K (in Ref. 6; AAD52031).
{ECO:0000305}.
CONFLICT 426 426 E -> D (in Ref. 6; AAD52031).
{ECO:0000305}.
CONFLICT 433 433 Missing (in Ref. 6; AAD52031).
{ECO:0000305}.
SEQUENCE 760 AA; 83284 MW; A3A2D92DF93D4F43 CRC64;
MAMTPVASSS PVSTCRLFRC NLLPDLLPKP LFLSLPKRNR IASCRFTVRA SANATVESPN
GVPASTSDTD TETDTTSYGR QFFPLAAVVG QEGIKTALLL GAVDREIGGI AISGRRGTAK
TVMARGLHEI LPPIEVVVGS ISNADPACPD EWEDDLDERI EYNADNTIKT EIVKSPFIQI
PLGVTEDRLI GSVDVEESVK RGTTVFQPGL LAEAHRGVLY VDEINLLDEG ISNLLLNVLT
DGVNIVEREG ISFRHPCKPL LIATYNPEEG AVREHLLDRV AINLSADLPM SFEDRVAAVG
IATQFQERCN EVFRMVNEET ETAKTQIILA REYLKDVKIS REQLKYLVLE AVRGGVQGHR
AELYAARVAK CLAAIEGREK VTIDDLRKAV ELVILPRSSL DETPPEQQNQ PPPPPPPPQN
SESGEEENEE EQEEEEEDES NEENENEQQQ DQIPEEFIFD AEGGLVDEKL LFFAQQAQKR
RGKAGRAKNV IFSEDRGRYI KPMLPKGPVK RLAVDATLRA AAPYQKLRRE KDISGTRKVF
VEKTDMRAKR MARKAGALVI FVVDASGSMA LNRMQNAKGA ALKLLAESYT SRDQVSIIPF
RGDAAEVLLP PSRSIAMARN RLERLPCGGG SPLAHGLTTA VRVGLNAEKS GDVGRIMIVA
ITDGRANITL KRSTDPESIA PDAPRPTSKE LKDEILEVAG KIYKAGMSLL VIDTENKFVS
TGFAKEIARV AQGKYYYLPN ASDAVISATT RDALSDLKNS


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