CHLD_ORYSI
ID CHLD_ORYSI Reviewed; 754 AA.
AC B8AMB8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 76.
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; ORFNames=OsI_14020;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
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 (By similarity).
CC {ECO:0000250}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000128; EEC76389.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AMB8; -.
DR SMR; B8AMB8; -.
DR STRING; 39946.B8AMB8; -.
DR EnsemblPlants; BGIOSGA013798-TA; BGIOSGA013798-PA; BGIOSGA013798.
DR Gramene; BGIOSGA013798-TA; BGIOSGA013798-PA; BGIOSGA013798.
DR HOGENOM; CLU_016684_6_2_1; -.
DR OMA; YYHLPKA; -.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000007015; Chromosome 3.
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 3: Inferred from homology;
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_0000418769"
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"
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
