HAMAP rule MF_00355
General rule information
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Accession | MF_00355 |
Dates | 1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 48) |
Name | ChlL_BchL |
Scope | Bacteria
Plastid |
Templates | Q9RFD6 (BCHL_CERS4); P0CY53 (BCHL_RHOCA); D5ANS3 (BCHL_RHOCB): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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case <OC:Bacteria> and not <OC:Cyanobacteriota>
Identifier |
|
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
Identifier |
|
end case
Protein name |
|
case <OC:Bacteria> and not <OC:Cyanobacteriota>
Gene name |
|
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
Gene name |
|
end case
Comments
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Function | Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. |
Catalytic activity | RHEA:28202: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
EC 1.3.7.7 |
case <FTGroup:1>
Cofactor | [4Fe-4S] cluster Note: Binds 1 [4Fe-4S] cluster per dimer. |
end case
case <OC:Bacteria> and not <OC:Cyanobacteriota>
Pathway | Porphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis (light-independent). |
Subunit | Homodimer. Protochlorophyllide reductase is composed of three subunits; BchL, BchN and BchB. |
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
Pathway | Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent). |
Subunit | Homodimer. Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. |
end case
case <OG:Chloroplast>
Subcellular location | Plastid, chloroplast. |
end case
Similarity | Belongs to the NifH/BchL/ChlL family. |
Keywords
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case <OC:Bacteria> and not <OC:Cyanobacteriota>
end case
case <FTGroup:1>
end case
Gene Ontology
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GO:0005524; Molecular function: ATP binding.
GO:0016636; Molecular function: oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor.
GO:0016636; Molecular function: oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor.
case <FTGroup:1>
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding.
end case
case <OC:Bacteria> and not <OC:Cyanobacteriota>
GO:0030494; Biological process: bacteriochlorophyll biosynthetic process.
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
GO:0015995; Biological process: chlorophyll biosynthetic process.
end case
GO:0015979; Biological process: photosynthesis.
case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case
Cross-references
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Pfam | PF00142; Fer4_NifH; 1; |
PIRSF | PIRSF000363; Nitrogenase_iron; 1; |
PRINTS | PR00091; NITROGNASEII; 1; |
NCBIfam | TIGR01281; DPOR_bchL; 1; |
PROSITE | PS00746; NIFH_FRXC_1; 1; |
PS00692; NIFH_FRXC_2; 1; | |
PS51026; NIFH_FRXC_3; 1; |
Features
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From: BCHL_CERS4 (Q9RFD6) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 41 | 46 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | G-[IV]-G-K-S-T | ||||||||
BINDING | 211 | 212 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | N-R | ||||||||
BINDING (Optional) | 235 | 237 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | P-x-L | ||||||||
BINDING | 45 | 45 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420 | S | ||||||||
BINDING | 126 | 126 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="ligand shared between dimeric partners | C | 1 | |||||||
BINDING | 160 | 160 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="ligand shared between dimeric partners | C | 1 | |||||||
BINDING | 70 | 70 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | K |
Additional information
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Size range | 245-331 amino acids |
Related rules | MF_00533 (NIFH) |
Fusion | None |
Comments | External expert: Yuichi Fujita, fujita@protein.osaka-u.ac.jp |