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Annotation rule MF_00353 |
General rule information
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Accession |
MF_00353 |
Dates |
1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 41) |
Propagated annotation
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Identifier, protein and gene names
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case <OC:Bacteria> and not <OC:Cyanobacteria>
end case
case <OC:Cyanobacteria> or <OG:Chloroplast>
end case
Protein name |
RecName:
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Full=Light-independent protochlorophyllide reductase subunit B;
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Short=DPOR subunit B;
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Short=LI-POR subunit B;
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EC 1.3.7.7;
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case <OC:Bacteria> and not <OC:Cyanobacteria>
end case
case <OC:Cyanobacteria> or <OG:Chloroplast>
end case
case <OC:Bacteria> and not <OC:Cyanobacteria>
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:Cyanobacteria> 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
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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. |
case <OC:Bacteria> and not <OC:Cyanobacteria>
end case
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:Cyanobacteria>
GO:0030494; Biological process: bacteriochlorophyll biosynthetic process.
end case
case <OC:Cyanobacteria> or <OG:Chloroplast>
GO:0015995; Biological process: chlorophyll biosynthetic process.
end case
case <OG:Chloroplast>
end case
From: BCHB_RHOCB (P26163) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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REGION
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409
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410
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Substrate binding
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G-[LM]
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ACT_SITE
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274
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274
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Proton donor
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D
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METAL
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36
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36
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Iron-sulfur (4Fe-4S); shared with heterodimeric partner
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D
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Additional information
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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. |