ID Q45KX6_HORVU Unreviewed; 761 AA.
AC Q45KX6;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513 {ECO:0000313|EMBL:AAZ32779.1};
RN [1] {ECO:0000313|EMBL:AAZ32779.1}
RP NUCLEOTIDE SEQUENCE.
RA Axelsson E.;
RT "Molecular explanation of five barley mutants defective in the D-subunit of
RT magnesium chelatase.";
RL Submitted (JUL-2005) 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}.
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DR EMBL; DQ125942; AAZ32779.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45KX6; -.
DR EnsemblPlants; HORVU.MOREX.r2.5HG0435780.1; HORVU.MOREX.r2.5HG0435780.1; HORVU.MOREX.r2.5HG0435780.
DR EnsemblPlants; HORVU.MOREX.r2.5HG0435780.1.mrna1; HORVU.MOREX.r2.5HG0435780.1.mrna1; HORVU.MOREX.r2.5HG0435780.1.
DR Gramene; HORVU.MOREX.r2.5HG0435780.1; HORVU.MOREX.r2.5HG0435780.1; HORVU.MOREX.r2.5HG0435780.
DR Gramene; HORVU.MOREX.r2.5HG0435780.1.mrna1; HORVU.MOREX.r2.5HG0435780.1.mrna1; HORVU.MOREX.r2.5HG0435780.1.
DR UniPathway; UPA00668; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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 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; SM00382; AAA; 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|ARBA:ARBA00023171,
KW 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|ARBA:ARBA00022531,
KW ECO:0000256|RuleBase:RU362087}; Plastid {ECO:0000256|RuleBase:RU362087}.
FT DOMAIN 559..759
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 399..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..420
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..452
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 82670 MW; 9FB0512609A5A6B5 CRC64;
MAAMATALST SLPHLPPRRL PSHPVAALSL APRGFRRREA PARLAAVASA SEVLDSTNGA
APAPTSPAPS GQQKYGREYF PLAAVVGQDA IKTSLLLGAI DREVGGIAIS GKRGTAKTVM
ARGLHAMLPP IEVVVGSIAN ADPNIPEEWE DHLADQVQYD ADGNVKCEIV KAPFVQIPLG
VTEDRLIGSV DVEQSVRSGT TVFQPGLLAE AHRGVLYVDE INLLDDGISN LLLNVLTEGV
NIVEREGISF RHPCKPLLIA TYNPEEGSVR EHLLDRIAIN LSADLPLSFD DRVAAVNIAT
QFQESSKDVF KMVEEETEVA KTQIILAREY LKDVAISTEQ LKYLVMEAIR GGCQGHRAEL
YAARVAKCLA AMEGREKVFA EDLKKAVELV ILPRSIISDN PQEQQNQPPP PPPPPPPQNQ
DNAEDQDEKE EDEEKDEEEK EDDDEENEKQ DDQIPEEFIF DAEGGLVDDK LLFFAQQAQR
KKGKAGRAKN VIFSEDRGRY IKPMLPKGPV RRLAVDATLR AAAPYQKLRR EKSLDKTRKV
FVEKTDMRAK RMARKAGALV IFVVDASGSM ALNRMQNAKG AALKLLAESY TSRDQVAIIP
FRGDYAEVLL PPSRSIAMAR KRLEKLPCGG GSPLAHGLST AVRVGLNAEK SGDVGRIMIV
AITDGRANVS LKKSNDPEAA AASDAPRPST QELKDEILDV SAKIFKAGMS LLVIDTENKF
VSTGFAKEIA RVAQGKYYYL PNASDAVISA ATKTALADLK S
//
