Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Molybdopterin synthase sulfur carrier subunit

Gene

moaD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.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.

GO - Molecular functioni

GO - Biological processi

  • Mo-molybdopterin cofactor biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11597-MONOMER.
ECOL316407:JW0767-MONOMER.
MetaCyc:EG11597-MONOMER.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin synthase sulfur carrier subunit
Alternative name(s):
MPT synthase subunit 1
Molybdenum cofactor biosynthesis protein D
Molybdopterin-converting factor small subunit
Molybdopterin-converting factor subunit 1
Sulfur carrier protein MoaD
Gene namesi
Name:moaD
Synonyms:chlA4, chlM
Ordered Locus Names:b0784, JW0767
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11597. moaD.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8181Molybdopterin synthase sulfur carrier subunitPRO_0000209131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 8111-thioglycine; alternate1 Publication
Modified residuei81 – 811Glycyl adenylate; alternate1 Publication
Cross-linki81 – 81Glycyl lysine isopeptide (Gly-Lys) (interchain with K-119 in MoaE)

Post-translational modificationi

C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by MoeB, then thiocarboxylated (-COSH) by IscS.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein

Proteomic databases

PaxDbiP30748.

Expressioni

Inductioni

By anaerobiosis, repressed by the molybdenum cofactor.

Interactioni

Subunit structurei

Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Forms a stable heterotetrameric complex of 2 MoaD and 2 MoeB during adenylation of MoaD by MoeB. During catalysis MoaD shuttles between the two heterotetrameric complexes.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
moaEP307497EBI-554366,EBI-554376

Protein-protein interaction databases

BioGridi4262177. 13 interactions.
DIPiDIP-10231N.
IntActiP30748. 16 interactions.
MINTiMINT-155528.
STRINGi511145.b0784.

Structurei

Secondary structure

1
81
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi8 – 147Combined sources
Beta strandi17 – 215Combined sources
Helixi28 – 369Combined sources
Helixi40 – 467Combined sources
Beta strandi52 – 554Combined sources
Beta strandi58 – 603Combined sources
Beta strandi71 – 755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FM0X-ray1.45D1-81[»]
1FMAX-ray1.58D1-81[»]
1JW9X-ray1.70D1-81[»]
1JWAX-ray2.90D1-81[»]
1JWBX-ray2.10D1-81[»]
1NVIX-ray1.90D1-81[»]
3BIIX-ray2.50D1-81[»]
ProteinModelPortaliP30748.
SMRiP30748. Positions 1-81.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30748.

Family & Domainsi

Sequence similaritiesi

Belongs to the MoaD family.Curated

Phylogenomic databases

eggNOGiENOG4105M00. Bacteria.
COG1977. LUCA.
HOGENOMiHOG000280988.
InParanoidiP30748.
KOiK03636.
OMAiRELVACD.
PhylomeDBiP30748.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR012675. Beta-grasp_dom.
IPR010034. Mopterin_su_1.
IPR016155. Mopterin_synth/thiamin_S_b.
IPR003749. ThiS/MoaD.
[Graphical view]
PfamiPF02597. ThiS. 1 hit.
[Graphical view]
SUPFAMiSSF54285. SSF54285. 1 hit.
TIGRFAMsiTIGR01682. moaD. 1 hit.

Sequencei

Sequence statusi: Complete.

P30748-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKVLFFAQV RELVGTDATE VAADFPTVEA LRQHMAAQSD RWALALEDGK
60 70 80
LLAAVNQTLV SFDHPLTDGD EVAFFPPVTG G
Length:81
Mass (Da):8,758
Last modified:November 1, 1997 - v2
Checksum:i1E0A440520EE82F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91Q → E AA sequence (PubMed:8514782).Curated
Sequence conflicti45 – 451A → R in CAA49864 (PubMed:8361352).Curated

Mass spectrometryi

Molecular mass is 8773.6±0.2 Da from positions 1 - 81. Determined by ESI. The measured mass is that of the thiolated protein.1 Publication
Molecular mass is 8757.0±1.0 Da from positions 1 - 81. Determined by ESI. 1 Publication
Molecular mass is 8744 Da from positions 1 - 81. Determined by ESI. 1 Publication
Molecular mass is 8744 Da from positions 1 - 81. Determined by API. 1 Publication
Molecular mass is 8760 Da from positions 1 - 81. Determined by API. The measured mass is that of the thiolated protein.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49864.1.
U00096 Genomic DNA. Translation: AAC73871.1.
AP009048 Genomic DNA. Translation: BAA35442.1.
PIRiH64814.
RefSeqiNP_415305.1. NC_000913.3.
WP_000598619.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73871; AAC73871; b0784.
BAA35442; BAA35442; BAA35442.
GeneIDi945398.
KEGGiecj:JW0767.
eco:b0784.
PATRICi32116769. VBIEscCol129921_0810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49864.1.
U00096 Genomic DNA. Translation: AAC73871.1.
AP009048 Genomic DNA. Translation: BAA35442.1.
PIRiH64814.
RefSeqiNP_415305.1. NC_000913.3.
WP_000598619.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FM0X-ray1.45D1-81[»]
1FMAX-ray1.58D1-81[»]
1JW9X-ray1.70D1-81[»]
1JWAX-ray2.90D1-81[»]
1JWBX-ray2.10D1-81[»]
1NVIX-ray1.90D1-81[»]
3BIIX-ray2.50D1-81[»]
ProteinModelPortaliP30748.
SMRiP30748. Positions 1-81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262177. 13 interactions.
DIPiDIP-10231N.
IntActiP30748. 16 interactions.
MINTiMINT-155528.
STRINGi511145.b0784.

Proteomic databases

PaxDbiP30748.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73871; AAC73871; b0784.
BAA35442; BAA35442; BAA35442.
GeneIDi945398.
KEGGiecj:JW0767.
eco:b0784.
PATRICi32116769. VBIEscCol129921_0810.

Organism-specific databases

EchoBASEiEB1554.
EcoGeneiEG11597. moaD.

Phylogenomic databases

eggNOGiENOG4105M00. Bacteria.
COG1977. LUCA.
HOGENOMiHOG000280988.
InParanoidiP30748.
KOiK03636.
OMAiRELVACD.
PhylomeDBiP30748.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:EG11597-MONOMER.
ECOL316407:JW0767-MONOMER.
MetaCyc:EG11597-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP30748.
PROiP30748.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR012675. Beta-grasp_dom.
IPR010034. Mopterin_su_1.
IPR016155. Mopterin_synth/thiamin_S_b.
IPR003749. ThiS/MoaD.
[Graphical view]
PfamiPF02597. ThiS. 1 hit.
[Graphical view]
SUPFAMiSSF54285. SSF54285. 1 hit.
TIGRFAMsiTIGR01682. moaD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMOAD_ECOLI
AccessioniPrimary (citable) accession number: P30748
Secondary accession number(s): P77422
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The cross-link is not seen in all structures of the MoaE-MoaD complex.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.