4.99.1.3: sirohydrochlorin cobaltochelatase

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For detailed information about sirohydrochlorin cobaltochelatase, go to the full flat file.

Word Map on EC 4.99.1.3

4.99.1.3

protoporphyrin

megaterium

typhimurium

chlorophyll

precorrin-2

uroporphyrinogen

tetrapyrrole

primordial

sirohaem

dehydrogenation

histidine-rich

epr

atp-independent

ferrochelation

Reaction

+ 2 H+ =

Synonyms

anaerobic cobalt chelatase, archaeal cobaltochelatase, CbiK, CbiKc, CbiKp, CbiX, CbiX0H, CbiXL, CbiXOH, CbiXS, cobalamin cobalt chelatase, cobalt chelatase, cobaltochelatase, More, sirohydrochlorin cobalt chelatase, sirohydrochlorin cobalt-lyase, sirohydrochlorin cobaltochelatase, sirohydrochlorin-ferrochelatase

ECTree

4 Lyases

4.99 Other lyases

4.99.1 Sole sub-subclass for lyases that do not belong in the other subclasses

4.99.1.3 sirohydrochlorin cobaltochelatase

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Results	in table
3327	AA Sequence
1	CAS Registry Number
16	Cloned(Commentary)
4	Cofactor
7	Crystallization (Commentary)
2	Expression
3	General Information
2	KM Value [mM]
12	Localization
8	Metals/Ions
26	Molecular Weight [Da]
32	Natural Substrates/ Products (Substrates)
49	Organism
1	Oxidation Stability
5	Pathway
34	PDB ID
6	Posttranslational Modification
32	Protein Variants
13	Purification (Commentary)
1	Reaction
37	Reference
24	Specific Activity [micromol/min/mg]
70	Substrates and Products (Substrate)
12	Subunits
90	Synonyms
1	Systematic Name

Subunits

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Subunits on EC 4.99.1.3 - sirohydrochlorin cobaltochelatase

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7 entries

oligomer

Brucella melitensis

x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT

699853

tetramer

3 entries

additional information

Brucella melitensis

the molecules are arranged in a two-tiered ring structure with the six subunits in each ring organized as a trimer of dimers, subunits CobS and CobT form a chaperone-like complex. Homology modelling of subunit CobS, overview

699853