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HAMAP rule MF_00353

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General rule information [?]

Accession MF_00353
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 46)
Name ChlB_BchB
Scope
Bacteria
Plastid
Templates P26163 (BCHB_RHOCB); P95463 (CHLB_LEPBY): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

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
bchB
end case
case <OC:Cyanobacteriota> or <OG:Chloroplast>
Gene name
chlB
end case

Comments [?]

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 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
Cofactor [4Fe-4S] cluster
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 [?]

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 [?]

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 <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 [?]

Pfam PF00148; Oxidored_nitro; 1;
PF08369; PCP_red; 1;
PIRSF PIRSF000163; PCP_ChlB; 1;
NCBIfam TIGR01278; DPOR_BchB; 1;

Features [?]

From: BCHB_RHOCB (P26163)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     409     410       /ligand="substrate     G-[LM]  
ACT_SITE     274     274       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 [?]

Size range 440-568 amino acids
Related rules None
Fusion 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.


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