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HAMAP rule MF_00785

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General rule information [?]

Accession MF_00785
Dates 24-MAY-2004 (Created)
19-NOV-2022 (Last updated, Version 29)
Name CbiX
Scope(s) Archaea
Template(s) O29537 (CBIX_ARCFU); O27448 (CFBA_METTH); P61816 (CFBA_METBF); Q8TJZ5 (CFBA_METAC); [ Recover all ]
Triggered by HAMAP; MF_00785 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
Identifier CFBA
Protein name RecName: Full=Sirohydrochlorin cobaltochelatase;
                 EC=4.99.1.3;
AltName: Full=CbiXS;
AltName: Full=Sirohydrochlorin nickelchelatase;
                 EC=4.99.1.11;
Gene name Name=cbiX; Synonyms=cfbA;
else
Identifier CBIX
Protein name RecName: Full=Sirohydrochlorin cobaltochelatase;
                 EC=4.99.1.3;
AltName: Full=CbiXS;
Gene name Name=cbiX;
end case

Comments [?]

case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
FUNCTIONCatalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin.
CATALYTIC ACTIVITY Reaction=Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin; Xref=Rhea:RHEA:15893, ChEBI:CHEBI:15378, ChEBI:CHEBI:48828, ChEBI:CHEBI:58351, ChEBI:CHEBI:60049; EC=4.99.1.3;
CATALYTIC ACTIVITY Reaction=2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin; Xref=Rhea:RHEA:52796, ChEBI:CHEBI:15378, ChEBI:CHEBI:49786, ChEBI:CHEBI:58351, ChEBI:CHEBI:136841; EC=4.99.1.11;
else
FUNCTIONCatalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
CATALYTIC ACTIVITY Reaction=Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin; Xref=Rhea:RHEA:15893, ChEBI:CHEBI:15378, ChEBI:CHEBI:48828, ChEBI:CHEBI:58351, ChEBI:CHEBI:60049; EC=4.99.1.3;
end case
PATHWAYCofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 1/10.
SUBUNITHomotetramer; dimer of dimers.
SIMILARITYBelongs to the CbiX family. CbiXS subfamily.

Keywords [?]

Cobalamin biosynthesis
Lyase
case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
Methanogenesis
end case
case <FT:2> and <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
Metal-binding
Cobalt
Nickel
else
Metal-binding
Cobalt
end case

Gene Ontology [?]

GO:0016852; Molecular function:sirohydrochlorin cobaltochelatase activity
GO:0019251; Biological process:anaerobic cobalamin biosynthetic process
case <FT:2> and <OCellular component:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
GO:0050897; Molecular function:cobalt ion binding
GO:0016151; Molecular function:nickel cation binding
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0050897; Molecular function:cobalt ion binding
end case

Cross-references [?]

Pfam PF01903; CbiX; 1;

Features [?]

From: CBIX_ARCFU (O29537)
Key From To Description Tag Condition FTGroup
BINDING 69 74 /ligand="substrate"
ACT_SITE 10 10 /note="Proton acceptor" H
case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
BINDING 10 10 /ligand="Co(2+)"
/ligand_id="ChEBI:CHEBI:48828"
H
BINDING 10 10 /ligand="Ni(2+)"
/ligand_id="ChEBI:CHEBI:49786"
H
BINDING 74 74 /ligand="Co(2+)"
/ligand_id="ChEBI:CHEBI:48828"
H
BINDING 74 74 /ligand="Ni(2+)"
/ligand_id="ChEBI:CHEBI:49786"
H
else
BINDING 10 10 /ligand="Co(2+)"
/ligand_id="ChEBI:CHEBI:48828"
H
BINDING 74 74 /ligand="Co(2+)"
/ligand_id="ChEBI:CHEBI:48828"
H
end case
BINDING 46 46 /ligand="substrate" [RKQE]

Additional information [?]

Size range 120-144 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments HALSA has a protein with two tandem copies of a cbiX domain, resembling CbiK arrangement.



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