CHLD_ORYSJ
ID CHLD_ORYSJ Reviewed; 754 AA.
AC Q6ATS0; A0A0P0W4J4; Q7XZG7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 CHLORINA 1;
DE Flags: Precursor;
GN Name=CHLD; Synonyms=CHL1; OrderedLocusNames=Os03g0811100, LOC_Os03g59640;
GN ORFNames=OsJ_13066, OSJNBa0028F23.2, OSJNBb0033J23.6;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, MUTAGENESIS OF ARG-393, AND DISRUPTION PHENOTYPE.
RX PubMed=16915519; DOI=10.1007/s11103-006-9024-z;
RA Zhang H., Li J., Yoo J.H., Yoo S.C., Cho S.H., Koh H.J., Seo H.S.,
RA Paek N.C.;
RT "Rice Chlorina-1 and Chlorina-9 encode ChlD and ChlI subunits of Mg-
RT chelatase, a key enzyme for chlorophyll synthesis and chloroplast
RT development.";
RL Plant Mol. Biol. 62:325-337(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP FUNCTION.
RX PubMed=22226678; DOI=10.1016/j.febslet.2011.12.026;
RA Zhou S., Sawicki A., Willows R.D., Luo M.;
RT "C-terminal residues of oryza sativa GUN4 are required for the activation
RT of the ChlH subunit of magnesium chelatase in chlorophyll synthesis.";
RL FEBS Lett. 586:205-210(2012).
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC The reaction takes place in two steps, with an ATP-dependent activation
CC followed by an ATP-dependent chelation step.
CC {ECO:0000269|PubMed:16915519, ECO:0000269|PubMed:22226678}.
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. {ECO:0000269|PubMed:16915519}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:16915519}.
CC -!- DISRUPTION PHENOTYPE: Homozygous KO plants are chlorotic lethal.
CC {ECO:0000269|PubMed:16915519}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP73850.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF065604; ABK58606.1; -; Genomic_DNA.
DR EMBL; EF065605; ABK58607.1; -; mRNA.
DR EMBL; AC135595; AAT77900.1; -; Genomic_DNA.
DR EMBL; AC137507; AAP73850.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF99490.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13582.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS87000.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE60156.1; -; Genomic_DNA.
DR EMBL; AK072463; BAG92983.1; -; mRNA.
DR RefSeq; XP_015631084.1; XM_015775598.1.
DR AlphaFoldDB; Q6ATS0; -.
DR SMR; Q6ATS0; -.
DR BioGRID; 803574; 1.
DR MINT; Q6ATS0; -.
DR STRING; 4530.OS03T0811100-01; -.
DR PaxDb; Q6ATS0; -.
DR PRIDE; Q6ATS0; -.
DR EnsemblPlants; Os03t0811100-01; Os03t0811100-01; Os03g0811100.
DR GeneID; 4334537; -.
DR Gramene; Os03t0811100-01; Os03t0811100-01; Os03g0811100.
DR KEGG; osa:4334537; -.
DR eggNOG; ENOG502QU3C; Eukaryota.
DR HOGENOM; CLU_016684_6_2_1; -.
DR InParanoid; Q6ATS0; -.
DR OMA; YYHLPKA; -.
DR OrthoDB; 918663at2759; -.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q6ATS0; baseline and differential.
DR Genevisible; Q6ATS0; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..754
FT /note="Magnesium-chelatase subunit ChlD, chloroplastic"
FT /id="PRO_0000418768"
FT DOMAIN 553..751
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..420
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 393
FT /note="R->Q: In chl1; yellowish-green leaf phenotype."
FT /evidence="ECO:0000269|PubMed:16915519"
SQ SEQUENCE 754 AA; 81879 MW; 8B9FAA055401164D CRC64;
MAMATTALSA SLPRLLPPRR RRFPTPSSSS PSAASTSTSR VVRLRAAAAS APSEVLDSTN
GAIPSGKGGG GQQYGREYFP LAAVVGQDAI KTALLLGAID REIGGIAISG KRGTAKTVMA
RGLHAMLPPI EVVVGSIANA DPNYPEEWEE GLANQVQYDA DGNLKTEIIK TPFVQIPLGI
TEDRLIGSVD VEASVKSGTT VFQPGLLAEA HRGVLYVDEI NLLDEGVSNL LLNVLTEGVN
IVEREGISFR HPCKPLLIAT YNPEEGSVRE HLLDRIAINL SADLPMSFDD RVAAVDIATQ
FQESSKEVFK MVEEETEVAK TQIILAREYL KDVAISTEQL KYLVMEAIRG GCQGHRAELY
AARVAKCLAA MEGREKVYVD DLKKAVELVI LPRSILSDNP QEQQDQQPPP PPPPPPPQDQ
DSQEDQDEDE EEDQEDDDEE NEQQDQQIPE EFIFDAEGGI VDEKLLFFAQ QAQRRRGKAG
RAKNLIFSSD RGRYIGSMLP KGPIRRLAVD ATLRAAAPYQ KLRREKDRDK TRKVFVEKTD
MRAKRMARKA GALVIFVVDA SGSMALNRMQ NAKGAALKLL AESYTSRDQV SIIPFRGDFA
EVLLPPSRSI AMARNRLEKL PCGGGSPLAH GLSTAVRVGL NAEKSGDVGR IMIVAITDGR
ANVSLKKSTD PEATSDAPRP SSQELKDEIL EVAGKIYKAG ISLLVIDTEN KFVSTGFAKE
IARVAQGKYY YLPNASDAVI SAATKTALSD LKSS
