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Q29PG5 (MOC32_DROPS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylyltransferase and sulfurtransferase MOCS3 2
Alternative name(s):
Molybdenum cofactor synthesis protein 3 2

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
ORF Names:GA12041
OrganismDrosophila pseudoobscura pseudoobscura (Fruit fly) [Reference proteome]
Taxonomic identifier46245 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays a central role in 2-thiolation of mcm5S2U 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 By similarity.

Catalytic activity

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

[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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.

Cofactor biosynthesis; molybdopterin biosynthesis.

Subcellular location

Cytoplasm › cytosol By similarity.

Sequence similarities

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

Contains 1 rhodanese domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Adenylyltransferase and sulfurtransferase MOCS3 2
PRO_0000369208

Regions

Domain353 – 44997Rhodanese
Nucleotide binding127 – 1315ATP By similarity
Nucleotide binding188 – 1892ATP By similarity

Sites

Active site2461Glycyl thioester intermediate; for adenylyltransferase activity By similarity
Active site4081Cysteine persulfide intermediate; for sulfurtransferase activity By similarity
Metal binding2291Zinc By similarity
Metal binding2321Zinc By similarity
Metal binding3041Zinc By similarity
Metal binding3071Zinc By similarity
Binding site991ATP; via amide nitrogen By similarity
Binding site1201ATP By similarity
Binding site1441ATP By similarity

Amino acid modifications

Modified residue601Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q29PG5 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 31E6FDE5E76538E3

FASTA45150,086
        10         20         30         40         50         60 
MIDSEALESE RVKLKRDIAD LRANLNRKEQ CLRELEAAIA AGEDSDEAEE SSNDMPTPQT 

        70         80         90        100        110        120 
KLTNDDIARY SRQLILQDFG VQGQLKLKNS SVLIVGMGGL GCPAAQYLVA AGCGHLGLID 

       130        140        150        160        170        180 
YDEVERSNLH RQILHSEHRC GMSKAESARI ALLELNSHCQ IRCHSRLINS MNAMHIIRPY 

       190        200        210        220        230        240 
DVVLDCSDNV ATRYLLNDAC VMLRKPLVSG SALKMDGQLT VYGYGQGPCY RCIYPVPPPP 

       250        260        270        280        290        300 
EAVTNCGDGG VLGAVTGIIG AMQALEAIKV IIGLGDVMSG RLLIFDGSSF MFRNIRIRTK 

       310        320        330        340        350        360 
RPNCHVCSAQ PLITELIDYE MFCGMHATDK DNPLDLLEPD QRLEVKEYHQ KLQSQPHLLL 

       370        380        390        400        410        420 
DVRPPAEFEI CQLPRSINVP LSEILDDSYL KRFAKQLEDK ELPIVLLCRR GNDSQIAVQH 

       430        440        450 
ITNRFPAHSI RDLVGGLHAW TGSVDATFPI Y

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH379058 Genomic DNA. Translation: EAL34328.1.
RefSeqXP_001357259.1. XM_001357223.2.

3D structure databases

ProteinModelPortalQ29PG5.
ModBaseSearch...

Protein-protein interaction databases

STRING7237.FBpp0279121.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0280683; FBpp0279121; FBgn0072089.
GeneID4817985.
KEGGdpo:Dpse_GA12041.

Organism-specific databases

FlyBaseFBgn0072089. Dpse\GA12041.

Phylogenomic databases

eggNOGCOG0476.
InParanoidQ29PG5.
KOK11996.
OMALCRYGND.
OrthoDBEOG4DNCKT.

Enzyme and pathway databases

UniPathwayUPA00344.
UPA00988.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR007901. 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. MoeB. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMOC32_DROPS
AccessionPrimary (citable) accession number: Q29PG5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 4, 2006
Last modified: April 3, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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