HAMAP rule MF_00355
General rule information
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| Accession | MF_00355 |
| Dates | 1-JUN-2001 (Created)
2-SEP-2024 (Last updated, Version 50) |
| Name | ChlL_BchL |
| Scope(s) |
Bacteria Plastid |
| Template(s) | Q9RFD6 (BCHL_CERS4); P0CY53 (BCHL_RHOCA); D5ANS3 (BCHL_RHOCB); [ Recover all ] |
| Triggered by |
HAMAP; MF_00355 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| case <OC:Bacteria> and not <OC:Cyanobacteriota> | |
| Identifier | BCHL |
| end case | |
| case <OC:Cyanobacteriota> or <OG:Chloroplast> | |
| Identifier | CHLL |
| end case | |
| Protein name | RecName: Full=Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein; Short=DPOR subunit L; Short=LI-POR subunit L; EC=1.3.7.7; |
| case <OC:Bacteria> and not <OC:Cyanobacteriota> | |
| Gene name | Name=bchL; |
| end case | |
| case <OC:Cyanobacteriota> or <OG:Chloroplast> | |
| Gene name | Name=chlL; |
| 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 | Reaction=chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 ADP + 2 phosphate = protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin] + 2 ATP + 2 H2O; Xref=Rhea:RHEA:28202, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723, ChEBI:CHEBI:43474, ChEBI:CHEBI:83348, ChEBI:CHEBI:83350, ChEBI:CHEBI:456216; EC=1.3.7.7; |
| case <FTGroup:1> | |
| COFACTOR | Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; 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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| Oxidoreductase | |
| Photosynthesis | |
| Chlorophyll biosynthesis | |
| case <OC:Bacteria> and not <OC:Cyanobacteriota> | |
| Bacteriochlorophyll biosynthesis | |
| end case | |
| ATP-binding | |
| Nucleotide-binding | |
| Magnesium | |
| Metal-binding | |
| case <FTGroup:1> | |
| Iron | |
| Iron-sulfur | |
| 4Fe-4S | |
| 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 | |
| case <FTGroup:1> | |
| GO:0051539; Molecular function:4 iron, 4 sulfur cluster binding | |
| end case | |
| case <OCellular component:Bacteria> and not <OC:Cyanobacteriota> | |
| GO:0036070; Biological process:light-independent bacteriochlorophyll biosynthetic process | |
| end case | |
| case <OCellular component:Cyanobacteriota> or <OG:Chloroplast> | |
| GO:0036068; Biological process:light-independent 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; |
| PROSITE | PS00692; NIFH_FRXC_2; 1; |
| PROSITE | 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 | 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 |
| Fusion | Nter: None Cter: None |
| Comments | External expert: Yuichi Fujita, fujita@protein.osaka-u.ac.jp |