CHLD_ARATH
ID CHLD_ARATH Reviewed; 760 AA.
AC Q9SJE1; B9DFK0; Q8GUL4; Q8VZU7; Q93YN7; Q9SWY5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Magnesium-chelatase subunit ChlD, chloroplastic;
DE Short=Mg-chelatase subunit D;
DE EC=6.6.1.1;
DE AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlD;
DE AltName: Full=Protein ALBINA 1;
DE AltName: Full=Protein PIGMENT DEFECTIVE EMBRYO 166;
DE Flags: Precursor;
GN Name=CHLD; Synonyms=ALB1, PDE166; OrderedLocusNames=At1g08520;
GN ORFNames=T27G7.20;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-441.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-759.
RC STRAIN=cv. C24;
RA Green J., Jensen P.E., Gibson L.C.D., Hunter C.N.;
RT "Characterization of the magnesium protoporphyrin chelatase chlD subunit
RT from Arabidopsis thaliana cv. c24.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19812694; DOI=10.1371/journal.pone.0007386;
RA Meinke D., Sweeney C., Muralla R.;
RT "Integrating the genetic and physical maps of Arabidopsis thaliana:
RT identification of mapped alleles of cloned essential (EMB) genes.";
RL PLoS ONE 4:E7386-E7386(2009).
RN [8]
RP INTERACTION WITH CHLI1 AND CHLD, AND FUNCTION.
RX PubMed=23011401; DOI=10.1007/s11103-012-9965-3;
RA Du S.Y., Zhang X.F., Lu Z., Xin Q., Wu Z., Jiang T., Lu Y., Wang X.F.,
RA Zhang D.P.;
RT "Roles of the different components of magnesium chelatase in abscisic acid
RT signal transduction.";
RL Plant Mol. Biol. 80:519-537(2012).
RN [9]
RP INDUCTION BY LIGHT.
RX PubMed=18846290; DOI=10.1039/b802596g;
RA Stephenson P.G., Terry M.J.;
RT "Light signalling pathways regulating the Mg-chelatase branchpoint of
RT chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.";
RL Photochem. Photobiol. Sci. 7:1243-1252(2008).
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and
CC CHLH. The reaction takes place in two steps, with an ATP-dependent
CC activation followed by an ATP-dependent chelation step. Does not bind
CC abscisic acid. {ECO:0000269|PubMed:19812694,
CC ECO:0000269|PubMed:23011401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-
CC protoporphyrin IX + phosphate; Xref=Rhea:RHEA:13961,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306,
CC ChEBI:CHEBI:60492, ChEBI:CHEBI:456216; EC=6.6.1.1;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: The magnesium chelatase complex is a heterotrimer consisting
CC of subunits CHLI, CHLD, AND CHLH. Interacts with CHLI1 and CHLH.
CC {ECO:0000269|PubMed:23011401}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- INDUCTION: Not regulated by light. {ECO:0000269|PubMed:18846290}.
CC -!- DISRUPTION PHENOTYPE: Pigment defective seeds and embryos.
CC {ECO:0000269|PubMed:19812694}.
CC -!- MISCELLANEOUS: Over-expression of CHLD has no impact on abscisic acid
CC sensitivity. {ECO:0000305|PubMed:23011401}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22895.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAO00766.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006932; AAF22895.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28301.1; -; Genomic_DNA.
DR EMBL; AY063821; AAL36177.1; -; mRNA.
DR EMBL; AY091402; AAM14341.1; -; mRNA.
DR EMBL; AK226535; BAE98674.1; -; mRNA.
DR EMBL; AK316801; BAH19517.1; -; mRNA.
DR EMBL; AF083555; AAD52031.1; -; mRNA.
DR EMBL; BT002406; AAO00766.1; ALT_INIT; mRNA.
DR EMBL; AY059906; AAL24388.1; -; mRNA.
DR EMBL; AY114693; AAM48012.1; -; mRNA.
DR PIR; B86218; B86218.
DR RefSeq; NP_563821.2; NM_100725.4.
DR AlphaFoldDB; Q9SJE1; -.
DR SMR; Q9SJE1; -.
DR BioGRID; 22615; 1.
DR STRING; 3702.AT1G08520.1; -.
DR PaxDb; Q9SJE1; -.
DR PRIDE; Q9SJE1; -.
DR ProteomicsDB; 246996; -.
DR EnsemblPlants; AT1G08520.1; AT1G08520.1; AT1G08520.
DR GeneID; 837374; -.
DR Gramene; AT1G08520.1; AT1G08520.1; AT1G08520.
DR KEGG; ath:AT1G08520; -.
DR Araport; AT1G08520; -.
DR TAIR; locus:2201796; AT1G08520.
DR eggNOG; ENOG502QU3C; Eukaryota.
DR HOGENOM; CLU_016684_6_2_1; -.
DR InParanoid; Q9SJE1; -.
DR OMA; YYHLPKA; -.
DR OrthoDB; 918663at2759; -.
DR PhylomeDB; Q9SJE1; -.
DR BioCyc; ARA:AT1G08520-MON; -.
DR BioCyc; MetaCyc:AT1G08520-MON; -.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q9SJE1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SJE1; baseline and differential.
DR Genevisible; Q9SJE1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0010007; C:magnesium chelatase complex; TAS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd01451; vWA_Magnesium_chelatase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041702; BchD/ChlD_VWA.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR TIGRFAMs; TIGR02031; BchD-ChlD; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chlorophyll biosynthesis; Chloroplast; Ligase;
KW Nucleotide-binding; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..760
FT /note="Magnesium-chelatase subunit ChlD, chloroplastic"
FT /id="PRO_0000002798"
FT DOMAIN 558..754
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 70
FT /note="D -> E (in Ref. 6; AAD52031)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> N (in Ref. 6; AAD52031)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="G -> S (in Ref. 6; AAD52031)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..286
FT /note="Missing (in Ref. 6; AAD52031)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="R -> S (in Ref. 6; AAD52031)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="E -> K (in Ref. 6; AAD52031)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="E -> D (in Ref. 6; AAD52031)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="Missing (in Ref. 6; AAD52031)"
FT /evidence="ECO:0000305"
SQ 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
