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Database: UniProt
Entry: A0A445D6W3_ARAHY
LinkDB: A0A445D6W3_ARAHY
Original site: A0A445D6W3_ARAHY 
ID   A0A445D6W3_ARAHY        Unreviewed;       708 AA.
AC   A0A445D6W3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE            EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN   ORFNames=Ahy_A05g024740 {ECO:0000313|EMBL:RYR58878.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR58878.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR58878.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR58878.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC       of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC       {ECO:0000256|RuleBase:RU362087}.
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         Evidence={ECO:0000256|ARBA:ARBA00001499,
CC         ECO:0000256|RuleBase:RU362087};
CC   -!- ACTIVITY REGULATION: Redox regulation; active in reducing conditions,
CC       inactive in oxidizing conditions. {ECO:0000256|RuleBase:RU362087}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00005173,
CC       ECO:0000256|RuleBase:RU362087}.
CC   -!- SUBUNIT: The magnesium chelatase complex is a heterotrimer consisting
CC       of subunits CHLI, CHLD, AND CHLH. {ECO:0000256|RuleBase:RU362087}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU362087}.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000256|ARBA:ARBA00005799, ECO:0000256|RuleBase:RU362087}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RYR58878.1}.
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DR   EMBL; SDMP01000005; RYR58878.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445D6W3; -.
DR   UniPathway; UPA00668; -.
DR   Proteomes; UP000289738; Chromosome a05.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd01451; vWA_Magnesium_chelatase; 1.
DR   Gene3D; 1.10.8.80; Magnesium chelatase subunit I, C-Terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
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   NCBIfam; TIGR02031; BchD-ChlD; 1.
DR   PANTHER; PTHR43473; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43473:SF2; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR   Pfam; PF17863; AAA_lid_2; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13519; VWA_2; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362087};
KW   Chlorophyll biosynthesis {ECO:0000256|RuleBase:RU362087};
KW   Chloroplast {ECO:0000256|RuleBase:RU362087};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU362087};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362087};
KW   Photosynthesis {ECO:0000256|RuleBase:RU362087};
KW   Plastid {ECO:0000256|RuleBase:RU362087};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT   DOMAIN          505..702
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          354..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..374
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..393
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   708 AA;  77491 MW;  6652F25CAC7B1159 CRC64;
     MGFALSLTLA APTFSNVPTL QSRSPLFCAM RFGSNNSRIQ RIRSESQNGA VVAAESEIPE
     SSNYGRHYFP LAAVVGQDAI KTALLLGAID PAIGGIAISD GLDQRVEYDS DGNVKTRIVK
     SPFVQIPLGV TEDRLIGSVD VEESVKTGTT VFQPGLLAEA HRGVLYVDEI NLLDEGISNL
     LLNVLTEGVN IVEREGISFK HPCRPLLIAT YNPEEGAVRE HLLDRVAINL SADLPMSFEE
     RVAAVGIATE FQEKSSQVFK MVEEETDSAK TQIILAREYL KDVSISREQL KYLVFEALRG
     DIQKLFELIG HRAELYAARV AKCLAALEGR DKVYVDDLKK AVELVILPRS IVSENPPEQQ
     NQQPPPPPPP PQNQEGDEQN EEEEQEDEND KENEQQQEQL PEEFIFDAEG GLVDEKLLFF
     AQQAQRRRGR AGRAKNVIFS EDRGRYIKPM LPKGPVKRLA VDATLRAAAP YQKLRRAKDS
     ESRRKVFVEK TDMRAKRMAR KAGALVIFVV DASGSMALNR MQNAKGAALK LLAESYTSRD
     QVSIIPFRGD AAEVLLPPSR SIAMARKRLE RLPCGGGSPL AHGLTTAVRV GLNAEKSGDV
     GRVMIVAITD GRANISLKRS TDPEAAAASD SPKPSAQDLK DEILEVAGKI YKAGMSLLVI
     DTENKFVSTG FAKEIARVAQ GKYYYLPNAS DAVISSATKD ALSALKNS
//
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