UniProt Accession

 MOCS3_HUMAN; O95396 

Genbank Protein ID

 AF102544; AL034553; BC015939 

Genbank Nucleotide ID

 AAC72412.1; CAB53750.1; AAH15939.1 

Protein Name

 Adenylyltransferase and sulfurtransferase MOCS3 

Protein Synonyms/Alias

 Molybdenum cofactor synthesis protein 3; Molybdopterin synthase sulfurylase; MPT synthase sulfurylase; Molybdopterin-synthase adenylyltransferase; Adenylyltransferase MOCS3; Sulfur carrier protein MOCS2A adenylyltransferase; Molybdopterin-synthase sulfurtransferase; Sulfur carrier protein MOCS2A sulfurtransferase; Sulfurtransferase MOCS3 

Gene Name

 MOCS3 

Gene Synonyms/Alias

 UBA4 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
27	ELNSLKQKLASALLA	ubiquitination	[1, 2]
137	EALAGQAKAFSAAAS	ubiquitination	[1]
342	RVSVTDYKRLLDSGA	ubiquitination	[1, 2]
376	HALHIPLKHLERRDA	ubiquitination	[2]
387	RRDAESLKLLKEAIW	ubiquitination	[2, 3, 4]
390	AESLKLLKEAIWEEK	ubiquitination	[2]
397	KEAIWEEKQGTQEGA	ubiquitination	[2]
413	VPIYVICKLGNDSQK	ubiquitination	[2]
423	NDSQKAVKILQSLSA	ubiquitination	[2]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. 

Sequence Annotation

 DOMAIN 347 458 Rhodanese.
 NP_BIND 120 124 ATP (By similarity).
 NP_BIND 181 182 ATP (By similarity).
 ACT_SITE 239 239 Glycyl thioester intermediate; for
 ACT_SITE 412 412 Cysteine persulfide intermediate; for
 METAL 222 222 Zinc (By similarity).
 METAL 225 225 Zinc (By similarity).
 METAL 297 297 Zinc (By similarity).
 METAL 300 300 Zinc (By similarity).
 BINDING 92 92 ATP; via amide nitrogen (By similarity).
 BINDING 113 113 ATP (By similarity).
 BINDING 137 137 ATP (By similarity).
 DISULFID 316 324 Alternate.  

Keyword

 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; Metal-binding; Molybdenum cofactor biosynthesis; Multifunctional enzyme; Nucleotide-binding; Polymorphism; Reference proteome; Transferase; tRNA processing; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 460 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
 GO:0004792; F:thiosulfate sulfurtransferase activity; IMP:UniProtKB.
 GO:0042292; F:URM1 activating enzyme activity; IDA:UniProtKB.
 GO:0018192; P:enzyme active site formation via L-cysteine persulfide; IDA:UniProtKB.
 GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:UniProtKB.
 GO:0034227; P:tRNA thio-modification; IDA:UniProtKB.
 GO:0002098; P:tRNA wobble uridine modification; IDA:UniProtKB.
 GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. 

Interpro

 IPR007901; MoeZ_MoeB.
 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR001763; Rhodanese-like_dom.
 IPR000594; ThiF_NAD_FAD-bd. 

Pfam

 PF05237; MoeZ_MoeB
 PF00581; Rhodanese
 PF00899; ThiF 

SMART

 SM00450; RHOD 

PROSITE

 PS50206; RHODANESE_3 

PRINTS