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Protein

Molybdopterin synthase catalytic subunit

Gene

moaE

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD.

Catalytic activityi

Cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + H2O = molybdopterin + 2 [molybdopterin-synthase sulfur-carrier protein].1 Publication

Pathwayi: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441Substrate
Binding sitei116 – 1161Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-2221-MONOMER.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin synthase catalytic subunit (EC:2.8.1.12)
Alternative name(s):
MPT synthase subunit 2
Molybdenum cofactor biosynthesis protein E
Molybdopterin-converting factor large subunit
Molybdopterin-converting factor subunit 2
Gene namesi
Name:moaE
Ordered Locus Names:SA2066
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 148148Molybdopterin synthase catalytic subunitPRO_0000163099Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Also stable as homodimer. The enzyme changes between these two forms during catalysis (By similarity).By similarity

Structurei

Secondary structure

1
148
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi14 – 207Combined sources
Beta strandi27 – 348Combined sources
Beta strandi39 – 424Combined sources
Beta strandi44 – 518Combined sources
Helixi53 – 7018Combined sources
Beta strandi75 – 817Combined sources
Beta strandi83 – 853Combined sources
Beta strandi90 – 10011Combined sources
Helixi101 – 11818Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi130 – 1334Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q5WX-ray2.00E1-148[»]
2QIEX-ray2.50A/E/H/K1-148[»]
ProteinModelPortaliP65401.
SMRiP65401. Positions 1-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP65401.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 363Substrate binding
Regioni100 – 1012Substrate binding
Regioni123 – 1253Substrate binding

Sequence similaritiesi

Belongs to the MoaE family.Curated

Phylogenomic databases

HOGENOMiHOG000280877.
OMAiSKDGSYW.
OrthoDBiEOG6KMBD9.

Family and domain databases

Gene3Di3.90.1170.40. 1 hit.
InterProiIPR003448. Mopterin_biosynth_MoaE.
[Graphical view]
PfamiPF02391. MoaE. 1 hit.
[Graphical view]
SUPFAMiSSF54690. SSF54690. 1 hit.

Sequencei

Sequence statusi: Complete.

P65401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQFEIVIEP IQTEQYREFT INEYQGAVVV FTGHVREWTK GVKTEYLEYE
60 70 80 90 100
AYIPMAEKKL AQIGDEINEK WPGTITSIVH RIGPLQISDI AVLIAVSSPH
110 120 130 140
RKDAYRANEY AIERIKEIVP IWKKEIWEDG SKWQGHQKGN YEEAKREE
Length:148
Mass (Da):17,351
Last modified:October 11, 2004 - v1
Checksum:iB4293AEE3AD0C030
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB43363.1.
PIRiB90025.
RefSeqiWP_000808495.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB43363; BAB43363; BAB43363.
PATRICi19576646. VBIStaAur116463_2241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB43363.1.
PIRiB90025.
RefSeqiWP_000808495.1. NC_002745.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q5WX-ray2.00E1-148[»]
2QIEX-ray2.50A/E/H/K1-148[»]
ProteinModelPortaliP65401.
SMRiP65401. Positions 1-136.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB43363; BAB43363; BAB43363.
PATRICi19576646. VBIStaAur116463_2241.

Phylogenomic databases

HOGENOMiHOG000280877.
OMAiSKDGSYW.
OrthoDBiEOG6KMBD9.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciSAUR158879:GJCB-2221-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP65401.

Family and domain databases

Gene3Di3.90.1170.40. 1 hit.
InterProiIPR003448. Mopterin_biosynth_MoaE.
[Graphical view]
PfamiPF02391. MoaE. 1 hit.
[Graphical view]
SUPFAMiSSF54690. SSF54690. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.
  2. "Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency."
    Daniels J.N., Wuebbens M.M., Rajagopalan K.V., Schindelin H.
    Biochemistry 47:615-626(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MOAD WITH OR WITHOUT PRECURSOR Z, CATALYTIC ACTIVITY, REACTION MECHANISM.
  3. Erratum
    Daniels J.N., Wuebbens M.M., Rajagopalan K.V., Schindelin H.
    Biochemistry 47:3315-3315(2008)

Entry informationi

Entry nameiMOAE_STAAN
AccessioniPrimary (citable) accession number: P65401
Secondary accession number(s): Q99S01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: March 16, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.