Summary: Molybdenum Cofactor Synthesis C
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Molybdenum Cofactor Synthesis C Provide feedback
This region contains two iron-sulphur (3Fe-4S) binding sites. Mutations in this region of O14940 cause MOCOD (Molybdenum Co-Factor Deficiency) type A.
Internal database links
SCOOP: | zf-C3HC4 zf-C3HC4_2 zf-C3HC4_3 zf-C3HC4_4 zf-RING_2 zf-RING_5 zf-RING_6 zf-RING_UBOX |
This tab holds annotation information from the InterPro database.
InterPro entry IPR010505
The majority of molybdenum-containing enzymes utilise a molybdenum cofactor (MoCF or Moco) consisting of a Mo atom coordinated via a cis-dithiolene moiety to molybdopterin (MPT). MoCF is ubiquitous in nature, and the pathway for MoCF biosynthesis is conserved in all three domains of life. MoCF-containing enzymes function as oxidoreductases in carbon, nitrogen, and sulphur metabolism [ PUBMED:16784786 , PUBMED:12114025 ].
In Escherichia coli, biosynthesis of MoCF is a three stage process. It begins with the MoaA and MoaC conversion of GTP to the meta-stable pterin intermediate precursor Z. The second stage involves MPT synthase (MoaD and MoaE), which converts precursor Z to MPT; MoeB is involved in the recycling of MPT synthase. The final step in MoCF synthesis is the attachment of mononuclear Mo to MPT, a process that requires MoeA and which is enhanced by MogA in an Mg2 ATP-dependent manner [ PUBMED:17198377 ]. MoCF is the active co-factor in eukaryotic and some prokaryotic molybdo-enzymes, but the majority of bacterial enzymes requiring MoCF, need a modification of MTP for it to be active; MobA is involved in the attachment of a nucleotide monophosphate to MPT resulting in the MGD co-factor, the active co-factor for most prokaryotic molybdo-enzymes. Bacterial two-hybrid studies have revealed the close interactions between MoeA, MogA, and MobA in the synthesis of MoCF [ PUBMED:12372836 ]. Moreover the close functional association of MoeA and MogA in the synthesis of MoCF is supported by fact that the known eukaryotic homologues to MoeA and MogA exist as fusion proteins: CNX1 ( SWISSPROT ) of Arabidopsis thaliana (Mouse-ear cress), mammalian Gephryin (e.g. SWISSPROT ) and Drosophila melanogaster (Fruit fly) Cinnamon ( SWISSPROT ) [ PUBMED:8528286 ].
This entry represents MoaA (also known as GTP 3',8-cyclase), which belongs to a family of enzymes involved in the synthesis of metallo-cofactors ( INTERPRO ). Each subunit of the MoaA dimer is comprised of an N-terminal SAM domain ( INTERPRO ) that contains the [4Fe-4S] cluster typical for this family of enzymes, as well as an additional [4Fe-4S] cluster in the C-terminal domain that is unique to MoaA proteins [ PUBMED:15317939 ]. The unique Fe site of the C-terminal [4Fe-4S] cluster is thought to be involved in the binding and activation of 5'-GTP.
Mutations in the human MoCF biosynthesis proteins MOCS1, MOCS2 or GEPH cause MoCF Deficiency type A (MOCOD), causing the loss of activity of MoCF-containing enzymes, resulting in neurological abnormalities and death [ PUBMED:12754701 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | molybdopterin synthase complex (GO:0019008) |
Molecular function | 4 iron, 4 sulfur cluster binding (GO:0051539) |
Biological process | Mo-molybdopterin cofactor biosynthetic process (GO:0006777) |
Domain organisation
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Alignments
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Seed (51) |
Full (7874) |
Representative proteomes | UniProt (35528) |
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RP15 (1030) |
RP35 (3656) |
RP55 (7710) |
RP75 (13203) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (51) |
Full (7874) |
Representative proteomes | UniProt (35528) |
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RP15 (1030) |
RP35 (3656) |
RP55 (7710) |
RP75 (13203) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation and family details
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Curation
Seed source: | ADDA_4938 |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Yeats C |
Number in seed: | 51 |
Number in full: | 7874 |
Average length of the domain: | 127.90 aa |
Average identity of full alignment: | 32 % |
Average coverage of the sequence by the domain: | 34.16 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 128 | ||||||||||||
Family (HMM) version: | 15 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 Mob_synth_C domain has been found. There are 8 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 sequence.
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