MOCS3

MOCS3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3I2V
Identifiers
Aliases	MOCS3 , UBA4, molybdenum cofactor synthesis 3
External IDs	OMIM: 609277 MGI: 1916622 HomoloGene: 6108 GeneCards: MOCS3
Gene location (Human)
Chr.	Chromosome 20 (human)
End	50,963,929 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	168,074,514 bp
RNA expression pattern
	Top expressed in
	sperm; ; Stromal cell of endometrium; ; ganglionic eminence; ; islet of Langerhans; ; gastrocnemius muscle; ; prefrontal cortex; ; bronchial epithelial cell; ; Left adrenal gland; ; right lobe of liver; ; right coronary artery;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity ; nucleotide binding ; thiosulfate sulfurtransferase activity ; molybdopterin-synthase sulfurtransferase activity ; metal ion binding ; URM1 activating enzyme activity ; GO:0001948, GO:0016582 protein binding ; catalytic activity ; ubiquitin-like modifier activating enzyme activity ; ATP binding ; molybdopterin-synthase adenylyltransferase activity ; nucleotidyltransferase activity ; sulfurtransferase activity ;
Cellular component	cytoplasm ; cytosol ;
Biological process	molybdopterin cofactor biosynthetic process ; tRNA processing ; Mo-molybdopterin cofactor biosynthetic process ; metabolism ; tRNA wobble uridine modification ; tRNA thio-modification ; tRNA wobble position uridine thiolation ; protein urmylation ;
	Sources:Amigo / QuickGO
Orthologs
	27304
	69372
	ENSG00000124217
	ENSMUSG00000074576
	O95396
	A2BDX3
	NM_014484
	NM_001160330
	NP_055299
	NP_001153802
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated July 17, 2022

Adenylyltransferase and sulfurtransferase MOCS3 is an enzyme that in humans is encoded by the MOCS3 gene.^[5]^[6]

Molybdenum cofactor (MoCo) is necessary for the function of all molybdoenzymes. One of the enzymes required for the biosynthesis of MoCo is molybdopterin synthase (MPT synthase, encoded by MOCS2 /Mocs2 in mammals). The protein encoded by this gene adenylates and activates MPT synthase. This gene contains no introns. A pseudogene of this gene is present on chromosome 14.^[6]

Related Research Articles

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Molybdopterins are a class of cofactors found in most molybdenum-containing and all tungsten-containing enzymes. Synonyms for molybdopterin are: MPT and pyranopterin-dithiolate. The nomenclature for this biomolecule can be confusing: Molybdopterin itself contains no molybdenum; rather, this is the name of the ligand that will bind the active metal. After molybdopterin is eventually complexed with molybdenum, the complete ligand is usually called molybdenum cofactor.

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Pterin-4-alpha-carbinolamine dehydratase is an enzyme that in humans is encoded by the PCBD1 gene.

Molybdenum cofactor biosynthesis protein 1 is a protein that in humans and other animals, fungi, and cellular slime molds, is encoded by the MOCS1 gene.

Molybdenum cofactor synthesis protein 2A and molybdenum cofactor synthesis protein 2B are a pair of proteins that in humans are encoded from the same MOCS2 gene. These two proteins dimerize to form molybdopterin synthase.

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in humans is encoded by the B3GAT3 gene.

Decaprenyl-diphosphate synthase subunit 1 is an enzyme that in humans is encoded by the PDSS1 gene.

Delta-aminolevulinate synthase 1 also known as ALAS1 is a protein that in humans is encoded by the ALAS1 gene. ALAS1 is an aminolevulinic acid synthase.

Molybdopterin synthase (EC 2.8.1.12, MPT synthase) is an enzyme required to synthesize molybdopterin (MPT) from precursor Z (now known as cyclic pyranopterin monophosphate). Molydopterin is subsequently complexed with molybdenum to form molybdenum cofactor (MoCo). MPT synthase catalyses the following chemical reaction:

Molybdopterin adenylyltransferase is an enzyme with systematic name ATP:molybdopterin adenylyltransferase. This enzyme catalyses the following chemical reaction

Molybdenum cofactor cytidylyltransferase is an enzyme with systematic name CTP:molybdenum cofactor cytidylyltransferase. This enzyme catalyses the following chemical reaction:

Molybdenum cofactor guanylyltransferase is an enzyme with systematic name GTP:molybdenum cofactor guanylyltransferase. This enzyme catalyses the following chemical reaction:

Molybdopterin-synthase adenylyltransferase is an enzyme with systematic name ATP:molybdopterin-synthase adenylyltransferase. This enzyme catalyses the following chemical reaction

Molybdopterin synthase sulfurtransferase is an enzyme with systematic name persulfurated L-cysteine desulfurase:(molybdopterin-synthase sulfur-carrier protein)-Gly-Gly sulfurtransferase. This enzyme catalyses the following chemical reaction

Cyclic pyranopterin monophosphate synthase is an enzyme with systematic name GTP 8,9-lyase . This enzyme catalyses the following chemical reaction

Mitochondrial amidoxime-reducing component 1 is a mammalian molybdenum-containing enzyme. It is located in the outer mitochondrial membrane and consists of a N-terminal mitochondrial signal domain facing the inter-membrane space, a transmembrane domain, and a C-terminal catalytic domain facing the cytosol. In humans it is encoded by the MOSC1 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000124217 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000074576 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Matthies A, Nimtz M, Leimkuhler S (May 2005). "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry". Biochemistry. 44 (21): 7912–20. doi:10.1021/bi0503448. PMID 15910006.
1 2 "Entrez Gene: MOCS3 molybdenum cofactor synthesis 3".

Reiss J, Johnson JL (2003). "Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and GEPH". Hum. Mutat. 21 (6): 569–76. doi:10.1002/humu.10223. PMID 12754701. S2CID 41013043.
Johnson JL, Coyne KE, Rajagopalan KV, et al. (2002). "Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency". Am. J. Med. Genet. 104 (2): 169–73. doi:10.1002/1096-8628(20011122)104:2<169::AID-AJMG1603>3.0.CO;2-8. PMID 11746050.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi: 10.1038/414865a . PMID 11780052.
Cortese MS, Caplan AB, Crawford RL (2003). "Structural, functional, and evolutionary analysis of moeZ, a gene encoding an enzyme required for the synthesis of the Pseudomonas metabolite, pyridine-2,6-bis(thiocarboxylic acid)". BMC Evol. Biol. 2: 8. doi:10.1186/1471-2148-2-8. PMC 115864 . PMID 11972321.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S (2004). "Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5946–51. Bibcode:2004PNAS..101.5946M. doi: 10.1073/pnas.0308191101 . PMC 395903 . PMID 15073332.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147 . PMID 15231747.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Krepinsky K, Leimkühler S (2007). "Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs". FEBS J. 274 (11): 2778–87. doi: 10.1111/j.1742-4658.2007.05811.x . PMID 17459099. S2CID 82541137.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000124217 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000074576 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid15910006-5] Matthies A, Nimtz M, Leimkuhler S (May 2005). "Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry". Biochemistry. 44 (21): 7912–20. doi:10.1021/bi0503448. PMID 15910006.

[entrez-6] 1 2 "Entrez Gene: MOCS3 molybdenum cofactor synthesis 3".

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MOCS3

Related Research Articles

References

Further reading