HAMAP rule MF_00353
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00353 |
| Accession | MF_00353 |
| Dates | 1-JUN-2001 (Created)
2-SEP-2024 (Last updated, Version 48) |
| Name | ChlB_BchB |
| Scope(s) |
Bacteria Plastid |
| Template(s) | P26163 (BCHB_RHOCB); P95463 (CHLB_LEPBY); [ Recover all ] |
| Triggered by |
HAMAP; MF_00353 (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 | BCHB |
| end case | |
| case <OC:Cyanobacteriota> or <OG:Chloroplast> | |
| Identifier | CHLB |
| end case | |
| Protein name | RecName: Full=Light-independent protochlorophyllide reductase subunit B; Short=DPOR subunit B; Short=LI-POR subunit B; EC=1.3.7.7; |
| case <OC:Bacteria> and not <OC:Cyanobacteriota> | |
| Gene name | Name=bchB; |
| end case | |
| case <OC:Cyanobacteriota> or <OG:Chloroplast> | |
| Gene name | Name=chlB; |
| end case | |
Comments
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| case <OC:Bacteria> and not <OC:Cyanobacteriota> | |
| 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 NB-protein (BchN-BchB) is the catalytic component of the complex. |
| PATHWAY | Porphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis (light-independent). |
| SUBUNIT | Protochlorophyllide reductase is composed of three subunits; BchL, BchN and BchB. Forms a heterotetramer of two BchB and two BchN subunits. |
| end case | |
| case <OC:Cyanobacteriota> or <OG:Chloroplast> | |
| 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 NB-protein (ChlN-ChlB) is the catalytic component of the complex. |
| PATHWAY | Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent). |
| SUBUNIT | Protochlorophyllide reductase is composed of three subunits; ChlL, ChlN and ChlB. Forms a heterotetramer of two ChlB and two ChlN subunits. |
| end case | |
| 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; |
| COFACTOR | Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.; |
| case <OG:Chloroplast> | |
| SUBCELLULAR LOCATION | Plastid, chloroplast. |
| end case | |
| SIMILARITY | Belongs to the ChlB/BchB/BchZ family. |
Keywords
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| ATP-binding | |
| Chlorophyll biosynthesis | |
| case <OC:Bacteria> and not <OC:Cyanobacteriota> | |
| Bacteriochlorophyll biosynthesis | |
| end case | |
| 4Fe-4S | |
| Iron | |
| Iron-sulfur | |
| Metal-binding | |
| Nucleotide-binding | |
| Oxidoreductase | |
| Photosynthesis | |
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:0051539; Molecular function:4 iron, 4 sulfur cluster binding | |
| 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 | PF00148; Oxidored_nitro; 1; |
| Pfam | PF08369; PCP_red; 1; |
| PIRSF | PIRSF000163; PCP_ChlB; 1; |
| NCBIfam | TIGR01278; DPOR_BchB; 1; |
Features
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| From: BCHB_RHOCB (P26163) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 409 | 410 | /ligand="substrate" | G-[LM] | ||||||||
| ACT_SITE | 274 | 274 | /note="Proton donor" | D | ||||||||
| BINDING | 36 | 36 | /ligand="[4Fe-4S] cluster" /ligand_id="ChEBI:CHEBI:49883" /ligand_note="ligand shared with heterodimeric partner" |
D | ||||||||
Additional information
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| Size range | 440-568 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | External expert: Yuichi Fujita, fujita@protein.osaka-u.ac.jp. Divergent chlamydomonadaceae (with insert) not shown in alignment and not used in size range. |