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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(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 [?]

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

Comments [?]

case <OC:Bacteria> and not <OC:Cyanobacteriota>
FUNCTIONComponent 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.
PATHWAYPorphyrin-containing compound metabolism; bacteriochlorophyll biosynthesis (light-independent).
SUBUNITProtochlorophyllide 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>
FUNCTIONComponent 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.
PATHWAYPorphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
SUBUNITProtochlorophyllide 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=2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe- 4S]-[ferredoxin]; 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 LOCATIONPlastid, chloroplast.
end case
SIMILARITYBelongs to the ChlB/BchB/BchZ family.

Keywords [?]


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 <OCellular component:Bacteria> and not <OC:Cyanobacteriota>
GO:0030494; Biological process:bacteriochlorophyll biosynthetic process
end case
case <OCellular component: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;
Pfam 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 /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 [?]

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.



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