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6  structures 1263  species 1  interaction 1426  sequences 8  architectures

Family: CysG_dimeriser (PF10414)

Summary: Sirohaem synthase dimerisation region

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This is the Wikipedia entry entitled "Sirohaem synthase". More...

Sirohaem synthase Edit Wikipedia article

CysG_dimerisation region
PDB 1pjq EBI.jpg
structure and function of cysg, the multifunctional methyltransferase/dehydrogenase/ferrochelatase for siroheme synthesis
Identifiers
Symbol CysG_dimeriser
Pfam PF10414
InterPro IPR019478

In molecular biology, sirohaem synthase (or siroheme synthase) (CysG) is a multi-functional enzyme with S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase, dehydrogenase and ferrochelatase activities. Bacterial sulphur metabolism depends on the iron-containing porphinoid sirohaem. CysG synthesizes sirohaem from uroporphyrinogen III via reactions which encompass two branchpoint intermediates in tetrapyrrole biosynthesis, diverting flux first from protoporphyrin IX biosynthesis and then from cobalamin (vitamin B12) biosynthesis. CysG is a dimer. Its dimerisation region is 74 amino acids long, and acts to hold the two structurally similar protomers held together asymmetrically through a number of salt-bridges across complementary residues within the dimerisation region.[1] CysG dimerisation produces a series of active sites, accounting for CysG's multi-functionality, catalysing four diverse reactions:

  • NAD+-dependent tetrapyrrole dehydrogenation

References[edit]

  1. ^ Stroupe ME, Leech HK, Daniels DS, Warren MJ, Getzoff ED (December 2003). "CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis". Nat. Struct. Biol. 10 (12): 1064–73. doi:10.1038/nsb1007. PMID 14595395. 

This article incorporates text from the public domain Pfam and InterPro IPR019478

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Sirohaem synthase dimerisation region Provide feedback

Bacterial sulfur metabolism depends on the iron-containing porphinoid sirohaem. CysG, S-adenosyl-L-methionine (SAM)-dependent bis-methyltransferase, dehydrogenase and ferrochelatase, synthesises sirohaem from uroporphyrinogen III via reactions which encompass two branchpoint intermediates in tetrapyrrole biosynthesis, diverting flux first from protoporphyrin IX biosynthesis and then from cobalamin (vitamin B12) biosynthesis. CysG is a dimer of two structurally similar protomers held together asymmetrically through a number of salt-bridges across complementary residues in the CysG_dimeriser region to produce a series of active sites, accounting for CysG's multifunctionality, catalysing four diverse reactions: two SAM-dependent methylations, NAD+-dependent tetrapyrrole dehydrogenation and metal chelation. The CysG_dimeriser region holding the two protomers together is of 74 residues [1].

Literature references

  1. Stroupe ME, Leech HK, Daniels DS, Warren MJ, Getzoff ED; , Nat Struct Biol. 2003;10:1064-1073.: CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis. PUBMED:14595395 EPMC:14595395


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR019478

Bacterial sulphur metabolism depends on the iron-containing porphinoid sirohaem. CysG is a multi-functional enzyme with S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase, dehydrogenase and ferrochelatase activities. CysG synthesizes sirohaem from uroporphyrinogen III via reactions which encompass two branchpoint intermediates in tetrapyrrole biosynthesis, diverting flux first from protoporphyrin IX biosynthesis and then from cobalamin (vitamin B12) biosynthesis. CysG is a dimer. Its dimerisation region is 74 residues long, and acts to hold the two structurally similar protomers held together asymmetrically through a number of salt-bridges across complementary residues within the dimerisation region [PUBMED:14595395]. CysG dimerisation produces a series of active sites, accounting for CysG's multi-functionality, catalysing four diverse reactions:

  • Two SAM-dependent methylations
  • NAD+-dependent tetrapyrrole dehydrogenation
  • Metal chelation

Gene Ontology

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Domain organisation

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Alignments

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(132)
Full
(1426)
Representative proteomes NCBI
(987)
Meta
(131)
RP15
(54)
RP35
(139)
RP55
(201)
RP75
(269)
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  Seed
(132)
Full
(1426)
Representative proteomes NCBI
(987)
Meta
(131)
RP15
(54)
RP35
(139)
RP55
(201)
RP75
(269)
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  Seed
(132)
Full
(1426)
Representative proteomes NCBI
(987)
Meta
(131)
RP15
(54)
RP35
(139)
RP55
(201)
RP75
(269)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Curation and family details

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Seed source: Gene3D, pdb_1pjq
Previous IDs: none
Type: Domain
Author: Finn RD, Coggill PC
Number in seed: 132
Number in full: 1426
Average length of the domain: 59.40 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 13.80 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.4 20.4
Trusted cut-off 20.4 20.4
Noise cut-off 20.0 20.2
Model length: 60
Family (HMM) version: 4
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Species distribution

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Interactions

There is 1 interaction for this family. More...

TP_methylase

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CysG_dimeriser domain has been found. There are 6 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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