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Protein

Adenylyltransferase and sulfurtransferase MOCS3

Gene

Mocs3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.UniRule annotation

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921ATP; via amide nitrogenUniRule annotation
Binding sitei113 – 1131ATPUniRule annotation
Binding sitei137 – 1371ATPUniRule annotation
Metal bindingi222 – 2221ZincUniRule annotation
Metal bindingi225 – 2251ZincUniRule annotation
Active sitei239 – 2391Glycyl thioester intermediate; for adenylyltransferase activityUniRule annotation
Metal bindingi297 – 2971ZincUniRule annotation
Metal bindingi300 – 3001ZincUniRule annotation
Active sitei412 – 4121Cysteine persulfide intermediate; for sulfurtransferase activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi120 – 1245ATPUniRule annotation
Nucleotide bindingi181 – 1822ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. molybdopterin-synthase adenylyltransferase activity Source: UniProtKB-EC
  4. molybdopterin-synthase sulfurtransferase activity Source: UniProtKB-EC
  5. nucleotidyltransferase activity Source: UniProtKB
  6. protein adenylyltransferase activity Source: GO_Central
  7. sulfurtransferase activity Source: UniProtKB
  8. thiosulfate sulfurtransferase activity Source: UniProtKB
  9. URM1 activating enzyme activity Source: UniProtKB

GO - Biological processi

  1. enzyme active site formation via L-cysteine persulfide Source: UniProtKB
  2. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB
  3. protein adenylylation Source: GOC
  4. protein urmylation Source: GO_Central
  5. tRNA thio-modification Source: UniProtKB
  6. tRNA wobble position uridine thiolation Source: GO_Central
  7. tRNA wobble uridine modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis, tRNA processing

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198541. Molybdenum cofactor biosynthesis.
UniPathwayiUPA00344.
UPA00988.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylyltransferase and sulfurtransferase MOCS3UniRule annotation
Alternative name(s):
Molybdenum cofactor synthesis protein 3UniRule annotation
Including the following 2 domains:
Molybdopterin-synthase adenylyltransferaseUniRule annotation (EC:2.7.7.80UniRule annotation)
Alternative name(s):
Adenylyltransferase MOCS3UniRule annotation
Sulfur carrier protein MOCS2A adenylyltransferaseUniRule annotation
Molybdopterin-synthase sulfurtransferaseUniRule annotation (EC:2.8.1.11UniRule annotation)
Alternative name(s):
Sulfur carrier protein MOCS2A sulfurtransferaseUniRule annotation
Sulfurtransferase MOCS3UniRule annotation
Gene namesi
Name:Mocs3
Synonyms:Uba4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1916622. Mocs3.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Adenylyltransferase and sulfurtransferase MOCS3PRO_0000281918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi316 ↔ 324AlternateUniRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiA2BDX3.
PaxDbiA2BDX3.
PRIDEiA2BDX3.

PTM databases

PhosphoSiteiA2BDX3.

Expressioni

Gene expression databases

BgeeiA2BDX3.
CleanExiMM_MOCS3.
ExpressionAtlasiA2BDX3. baseline and differential.
GenevestigatoriA2BDX3.

Interactioni

Subunit structurei

Interacts with NFS1.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096670.

Structurei

3D structure databases

ProteinModelPortaliA2BDX3.
SMRiA2BDX3. Positions 53-301, 335-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini347 – 458112RhodaneseUniRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.UniRule annotation
Contains 1 rhodanese domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00570000079161.
HOGENOMiHOG000281219.
HOVERGENiHBG052491.
InParanoidiA2BDX3.
KOiK11996.
OMAiSRRLDCA.
OrthoDBiEOG776SQ3.
TreeFamiTF106103.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_03049. MOCS3_Uba4.
InterProiIPR028885. 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]
PfamiPF05237. MoeZ_MoeB. 1 hit.
PF00581. Rhodanese. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2BDX3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPEDVAAL QAEITRREEE LASLKRRLAA ALTAEPEPER PLRVPPPPLA
60 70 80 90 100
PRAALSRDEI LRYSRQLLLP ELGVRGQLRL AAAAVLVVGC GGLGCPLAQY
110 120 130 140 150
LAAAGVGRLG LVDHDVVETS NLARQVLHGE AQAGESKARS AAAALRRLNS
160 170 180 190 200
AVECVAYPRA LAEDWALDLV RGYDVVADCC DNVPTRYLVN DACVLAGRPL
210 220 230 240 250
VSASALRFEG QMTVYHHDGG PCYRCVFPRP PPPETVTNCA DGGVLGAVPG
260 270 280 290 300
VLGCAQALEV LKIAAGLGSS YSGSMLLFDG LGGHFRRIRL RRRRPDCVVC
310 320 330 340 350
GQQPTVTRLQ DYEAFCGSSA TDKCRALKLL CPEERISVTD YKRLLDSGAP
360 370 380 390 400
HVLLDVRPQV EVDICRLPHS LHIPLSQLER RDADSLKLLG AALRKGKQES
410 420 430 440 450
QEGVALPVYV ICKLGNDSQK AVKVLQSLTA VPELDSLTVQ DIVGGLMAWA
460
AKIDGTFPQY
Length:460
Mass (Da):49,375
Last modified:February 20, 2007 - v1
Checksum:i7340FD4B2D9826F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX005039 Genomic DNA. Translation: CAM22977.1.
CCDSiCCDS50802.1.
RefSeqiNP_001153802.1. NM_001160330.1.
UniGeneiMm.482182.

Genome annotation databases

EnsembliENSMUST00000099071; ENSMUSP00000096670; ENSMUSG00000074576.
GeneIDi69372.
KEGGimmu:69372.
UCSCiuc012cjs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX005039 Genomic DNA. Translation: CAM22977.1.
CCDSiCCDS50802.1.
RefSeqiNP_001153802.1. NM_001160330.1.
UniGeneiMm.482182.

3D structure databases

ProteinModelPortaliA2BDX3.
SMRiA2BDX3. Positions 53-301, 335-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096670.

PTM databases

PhosphoSiteiA2BDX3.

Proteomic databases

MaxQBiA2BDX3.
PaxDbiA2BDX3.
PRIDEiA2BDX3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000099071; ENSMUSP00000096670; ENSMUSG00000074576.
GeneIDi69372.
KEGGimmu:69372.
UCSCiuc012cjs.1. mouse.

Organism-specific databases

CTDi27304.
MGIiMGI:1916622. Mocs3.

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00570000079161.
HOGENOMiHOG000281219.
HOVERGENiHBG052491.
InParanoidiA2BDX3.
KOiK11996.
OMAiSRRLDCA.
OrthoDBiEOG776SQ3.
TreeFamiTF106103.

Enzyme and pathway databases

UniPathwayiUPA00344.
UPA00988.
ReactomeiREACT_198541. Molybdenum cofactor biosynthesis.

Miscellaneous databases

NextBioi329269.
PROiA2BDX3.
SOURCEiSearch...

Gene expression databases

BgeeiA2BDX3.
CleanExiMM_MOCS3.
ExpressionAtlasiA2BDX3. baseline and differential.
GenevestigatoriA2BDX3.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_03049. MOCS3_Uba4.
InterProiIPR028885. 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]
PfamiPF05237. MoeZ_MoeB. 1 hit.
PF00581. Rhodanese. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiMOCS3_MOUSE
AccessioniPrimary (citable) accession number: A2BDX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: February 20, 2007
Last modified: February 4, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.