Enzyme

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     4. Lyases
        4.99 Other lyases
            4.99.1 Sole sub-subclass for lyases that do not belong in the other subclasses
ID:4.99.1.3
Description:Sirohydrochlorin cobaltochelatase.
Alternative Name: Cobaltochelatase.
Anaerobic cobalt chelatase.
Cath: 3.40.50.140; 3.40.50.1400;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.99.1.3
BRENDA Enzyme Link: BRENDA 4.99.1.3
KEGG Enzyme Link: KEGG4.99.1.3
BioCyc Enzyme Link: BioCyc 4.99.1.3
ExPASy Enzyme Link: ExPASy4.99.1.3
EC2PDB Enzyme Link: EC2PDB 4.99.1.3
ExplorEnz Enzyme Link: ExplorEnz 4.99.1.3
PRIAM enzyme-specific profiles Link: PRIAM 4.99.1.3
IntEnz Enzyme Link: IntEnz 4.99.1.3
MEDLINE Enzyme Link: MEDLINE 4.99.1.3
MSA:

4.99.1.3;

Phylogenetic Tree:

4.99.1.3;

Uniprot:
M-CSA:
RHEA:26269 Co-precorrin-2 + 3 H(+) = Co(2+) + precorrin-2
RULE(radius=1) [*:1]=[N+;H0:2](-[*:3])-[Co-2;H0:4]12-[N+;H0:5]3=[C;H0;+0:6](-[*:7]=[*:8]-[N;H0;+0:9]-1-[*:10])-[CH;+0:11](-[*:12])-[C;H0;+0:13](-[*:14])=[C;H0;+0:15]-3-[*:16]-[*:17]:[n;H0;+0:18]-2:[*:19].[H+;H0:20].[H+;H0:21].[H+;H0:22]>>([*:10]-[NH;+0:9]-[*:8]=[*:7]-[c;H0;+0:6]1:[nH;+0:5]:[c;H0;+0:15](-[*:16]-[*:17]:[nH;+0:18]:[*:19]):[c;H0;+0:13](-[*:14]):[c;H0;+0:11]:1-[*:12].[*:1]=[N;H0;+0:2]-[*:3]).[Co+2;H0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis.Schubert HL, Raux E, Wilson KS, Warren MJ1999 Aug 1710451360
A role for Salmonella typhimurium cbiK in cobalamin (vitamin B12) and siroheme biosynthesis.Raux E, Thermes C, Heathcote P, Rambach A, Warren MJ1997 May9150215

RHEA:15893 Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
RULE(radius=1) [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5]2=[N+;H0:6]3-[C;H0;+0:7]-1=[CH;+0:8]-[*:9]:[n;H0;+0:10]1:[*:11]-[CH;+0:12]=[C;H0;+0:13]4-[*:14]-[*:15]-[C;H0;+0:16]5=[N+;H0:17]-4-[Co-2;H0:18]-3-1-[N;H0;+0:19]1-[C;H0;+0:20](=[CH;+0:21]-5)-[*:22]-[*:23]-[C;H0;+0:24]-1=[CH;+0:25]-2.[H+;H0:26].[H+;H0:27]>>[*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5]2:[cH;+0:25]:[c;H0;+0:24]3:[nH;+0:19]:[c;H0;+0:20](:[cH;+0:21]:[c;H0;+0:16]4:[n;H0;+0:17]:[c;H0;+0:13](:[cH;+0:12]:[*:11]:[nH;+0:10]:[*:9]:[cH;+0:8]:[c;H0;+0:7]:1:[n;H0;+0:6]:2)-[*:14]-[*:15]-4)-[*:22]-[*:23]-3.[Co+2;H0:18]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
A story of chelatase evolution: identification and characterization of a small 13-15-kDa "ancestral" cobaltochelatase (CbiXS) in the archaea.Brindley AA, Raux E, Leech HK, Schubert HL, Warren MJ2003 Jun 2012686546
Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis.Schubert HL, Raux E, Wilson KS, Warren MJ1999 Aug 1710451360
The biosynthesis of adenosylcobalamin (vitamin B12).Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC2002 Aug12195810