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A2BDX3 (MOCS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylyltransferase and sulfurtransferase MOCS3
Alternative name(s):
Molybdenum cofactor synthesis protein 3

Including the following 2 domains:

  1. Molybdopterin-synthase adenylyltransferase
    EC=2.7.7.80
    Alternative name(s):
    Adenylyltransferase MOCS3
    Sulfur carrier protein MOCS2A adenylyltransferase
  2. Molybdopterin-synthase sulfurtransferase
    EC=2.8.1.11
    Alternative name(s):
    Sulfur carrier protein MOCS2A sulfurtransferase
    Sulfurtransferase MOCS3
Gene names
Name:Mocs3
Synonyms:Uba4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of cytosolic 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 By similarity. HAMAP-Rule MF_03049

Catalytic activity

ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP. HAMAP-Rule MF_03049

[Molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + cysteine desulfurase. HAMAP-Rule MF_03049

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_03049

Pathway

tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. HAMAP-Rule MF_03049

Cofactor biosynthesis; molybdopterin biosynthesis. HAMAP-Rule MF_03049

Subunit structure

Interacts with NFS1.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03049.

Sequence similarities

In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.

Contains 1 rhodanese domain.

Ontologies

Keywords
   Biological processMolybdenum cofactor biosynthesis
tRNA processing
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionTransferase
   PTMDisulfide bond
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processMo-molybdopterin cofactor biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme active site formation via L-cysteine persulfide

Inferred from sequence or structural similarity. Source: UniProtKB

tRNA thio-modification

Inferred from sequence or structural similarity. Source: UniProtKB

tRNA wobble position uridine thiolation

Inferred from electronic annotation. Source: InterPro

tRNA wobble uridine modification

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

URM1 activating enzyme activity

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

molybdopterin-synthase adenylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

molybdopterin-synthase sulfurtransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

nucleotidyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

sulfurtransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

thiosulfate sulfurtransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Adenylyltransferase and sulfurtransferase MOCS3 HAMAP-Rule MF_03049
PRO_0000281918

Regions

Domain347 – 458112Rhodanese
Nucleotide binding120 – 1245ATP By similarity
Nucleotide binding181 – 1822ATP By similarity

Sites

Active site2391Glycyl thioester intermediate; for adenylyltransferase activity By similarity
Active site4121Cysteine persulfide intermediate; for sulfurtransferase activity By similarity
Metal binding2221Zinc By similarity
Metal binding2251Zinc By similarity
Metal binding2971Zinc By similarity
Metal binding3001Zinc By similarity
Binding site921ATP; via amide nitrogen By similarity
Binding site1131ATP By similarity
Binding site1371ATP By similarity

Amino acid modifications

Disulfide bond316 ↔ 324Alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BDX3 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 7340FD4B2D9826F1

FASTA46049,375
        10         20         30         40         50         60 
MAAPEDVAAL QAEITRREEE LASLKRRLAA ALTAEPEPER PLRVPPPPLA PRAALSRDEI 

        70         80         90        100        110        120 
LRYSRQLLLP ELGVRGQLRL AAAAVLVVGC GGLGCPLAQY LAAAGVGRLG LVDHDVVETS 

       130        140        150        160        170        180 
NLARQVLHGE AQAGESKARS AAAALRRLNS AVECVAYPRA LAEDWALDLV RGYDVVADCC 

       190        200        210        220        230        240 
DNVPTRYLVN DACVLAGRPL VSASALRFEG QMTVYHHDGG PCYRCVFPRP PPPETVTNCA 

       250        260        270        280        290        300 
DGGVLGAVPG VLGCAQALEV LKIAAGLGSS YSGSMLLFDG LGGHFRRIRL RRRRPDCVVC 

       310        320        330        340        350        360 
GQQPTVTRLQ DYEAFCGSSA TDKCRALKLL CPEERISVTD YKRLLDSGAP HVLLDVRPQV 

       370        380        390        400        410        420 
EVDICRLPHS LHIPLSQLER RDADSLKLLG AALRKGKQES QEGVALPVYV ICKLGNDSQK 

       430        440        450        460 
AVKVLQSLTA VPELDSLTVQ DIVGGLMAWA AKIDGTFPQY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX005039 Genomic DNA. Translation: CAM22977.1.
RefSeqNP_001153802.1. NM_001160330.1.
UniGeneMm.482182.

3D structure databases

ProteinModelPortalA2BDX3.
SMRA2BDX3. Positions 53-301, 335-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000096670.

PTM databases

PhosphoSiteA2BDX3.

Proteomic databases

PaxDbA2BDX3.
PRIDEA2BDX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099071; ENSMUSP00000096670; ENSMUSG00000074576.
GeneID69372.
KEGGmmu:69372.
UCSCuc012cjs.1. mouse.

Organism-specific databases

CTD27304.
MGIMGI:1916622. Mocs3.

Phylogenomic databases

eggNOGCOG0476.
GeneTreeENSGT00570000079161.
HOGENOMHOG000281219.
HOVERGENHBG052491.
InParanoidA2BDX3.
KOK11996.
OMAEAFCGSS.
OrthoDBEOG776SQ3.
TreeFamTF106103.

Enzyme and pathway databases

UniPathwayUPA00344.
UPA00988.

Gene expression databases

ArrayExpressA2BDX3.
BgeeA2BDX3.
CleanExMM_MOCS3.
GenevestigatorA2BDX3.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_03049. MOCS3_Uba4.
InterProIPR028885. MOCS3/Uba4.
IPR007901. MoeZ_MoeB.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR001763. Rhodanese-like_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamPF05237. MoeZ_MoeB. 1 hit.
PF00581. Rhodanese. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio329269.
PROA2BDX3.
SOURCESearch...

Entry information

Entry nameMOCS3_MOUSE
AccessionPrimary (citable) accession number: A2BDX3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: February 20, 2007
Last modified: April 16, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot