Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9ZNW0 (MOCS3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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 13
    Short name=AtStr13
    Sulfurtransferase MOCS3
Gene names
Name:MOCS3
Synonyms:CNX5, STR13, UBA4
Ordered Locus Names:At5g55130
ORF Names:MCO15.8
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length464 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 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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9ZNW0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9ZNW0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     85-111: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Adenylyltransferase and sulfurtransferase MOCS3
PRO_0000120584

Regions

Domain358 – 462105Rhodanese
Nucleotide binding129 – 1335ATP By similarity
Nucleotide binding190 – 1912ATP By similarity

Sites

Active site2481Glycyl thioester intermediate; for adenylyltransferase activity By similarity
Active site4221Cysteine persulfide intermediate; for sulfurtransferase activity By similarity
Metal binding2311Zinc By similarity
Metal binding2341Zinc By similarity
Metal binding3061Zinc By similarity
Metal binding3091Zinc By similarity
Binding site1011ATP; via amide nitrogen By similarity
Binding site1221ATP By similarity
Binding site1461ATP By similarity

Natural variations

Alternative sequence85 – 11127Missing in isoform 2.
VSP_042632

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 844C7C35C7737940

FASTA46450,574
        10         20         30         40         50         60 
MMSNGGDSSE IVRELEELKL KKAEIEHRIS TLEAKLQDTA AVELYDAVSN GDSYLTAPEL 

        70         80         90        100        110        120 
EHGLSPDQIY RYSRQLLLPS FAVEGQSNLL KSSVLVIGAG GLGSPALLYL AACGVGQLGI 

       130        140        150        160        170        180 
IDHDVVELNN MHRQIIHTEA FIGHPKVKSA AAACRSINST IKVDEYVEAL RTSNALEILS 

       190        200        210        220        230        240 
QYDIIVDATD NPPSRYMISD CCVLLGKPLV SGAALGMEGQ LTVYNHNGGP CYRCLFPTPP 

       250        260        270        280        290        300 
PTSACQRCSD SGVLGVVPGV IGCLQALETI KLASLVGEPL SERMLLFDAL SARMRIVKIR 

       310        320        330        340        350        360 
GRSSQCTVCG DNSSFNKQTF KDFDYEDFTQ FPLFAGPLNL LPAESRISSK EFKEILQKKE 

       370        380        390        400        410        420 
QHVLLDVRPS HHYKIVSLPD SLNIPLANLE TRLNELTSAL KEKGNGHANT ESCTNPSVFV 

       430        440        450        460 
VCRRGNDSQR AVQYLRESGF DSAKDIIGGL EAWAANVNPN FPTY

« Hide

Isoform 2 [UniParc].

Checksum: D25E7E843FE21E11
Show »

FASTA43747,993

References

« Hide 'large scale' references
[1]"Isolation and sequencing of a genomic region coding for the MPT-synthase-sulphurylase (Cnx5) in A.thaliana."
Nieder J., Gutzke G., Mendel R.R.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"Molybdenum cofactor biosynthesis: identification of A.thaliana cDNAs homologous to the E.coli sulfotransferase MoeB."
Nieder J., Stallmeyer B., Brinkmann H., Mendel R.R.
(In) Cram W.J., de Kok L.J., Stulen I., Brunold C., Rennenberg H. (eds.); Sulphur Metabolism in Higher Plants, pp.275-277, Backhuys Publishers, Leiden (1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[6]"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
Tissue: Rosette leaf.
[7]"Differential expression of Arabidopsis sulfurtransferases under various growth conditions."
Bartels A., Mock H.P., Papenbrock J.
Plant Physiol. Biochem. 45:178-187(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF124160 Genomic DNA. Translation: AAD18051.1.
AF124159 mRNA. Translation: AAD18050.1.
AB010071 Genomic DNA. Translation: BAB08582.1.
CP002688 Genomic DNA. Translation: AED96586.1.
CP002688 Genomic DNA. Translation: AED96587.1.
BT029156 mRNA. Translation: ABJ17091.1.
AK317295 mRNA. Translation: BAH19971.1.
IPIIPI00524834.
RefSeqNP_001032076.1. NM_001036999.1.
NP_200324.1. NM_124895.2.
UniGeneAt.24643.
At.48080.

3D structure databases

ProteinModelPortalQ9ZNW0.
SMRQ9ZNW0. Positions 28-310, 345-464.
ModBaseSearch...

Proteomic databases

PaxDbQ9ZNW0.
PRIDEQ9ZNW0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G55130.1; AT5G55130.1; AT5G55130.
GeneID835604.
KEGGath:AT5G55130.

Organism-specific databases

TAIRAt5g55130.

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000281219.
InParanoidQ9ZNW0.
KOK11996.
OMAVIHGTSW.
PhylomeDBQ9ZNW0.
ProtClustDBCLSN2686972.

Enzyme and pathway databases

UniPathwayUPA00344.
UPA00988.

Gene expression databases

ArrayExpressQ9ZNW0.
GenevestigatorQ9ZNW0.

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.
PROSITEPS00380. RHODANESE_1. False negative.
PS00683. RHODANESE_2. False negative.
PS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMOCS3_ARATH
AccessionPrimary (citable) accession number: Q9ZNW0
Secondary accession number(s): B9DGV4, Q058R2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents