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: -Experimental evidence at protein leveli

Functioni

Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.1 Publication

Miscellaneous

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

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

Keywordsi

Biological processMolybdenum cofactor biosynthesis
LigandNucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11597-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11597 moaD

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002091311 – 81Molybdopterin synthase sulfur carrier subunitAdd BLAST81

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei811-thioglycine; alternate1 Publication1
Modified residuei81Glycyl adenylate; alternate1 Publication1
Cross-linki81Glycyl 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
PRIDEiP30748

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

Show more details

Protein-protein interaction databases

BioGridi4262177, 13 interactors
DIPiDIP-10231N
IntActiP30748, 16 interactors
STRINGi316385.ECDH10B_0852

Structurei

Secondary structure

181
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi8 – 14Combined sources7
Beta strandi17 – 21Combined sources5
Helixi28 – 36Combined sources9
Helixi40 – 46Combined sources7
Beta strandi52 – 55Combined sources4
Beta strandi58 – 60Combined sources3
Beta strandi71 – 75Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30748

Family & Domainsi

Sequence similaritiesi

Belongs to the MoaD family.Curated

Phylogenomic databases

eggNOGiENOG4105M00 Bacteria
COG1977 LUCA
HOGENOMiHOG000280988
InParanoidiP30748
KOiK03636
OMAiYAFENEG
PhylomeDBiP30748

Family and domain databases

Gene3Di3.10.20.30, 1 hit
InterProiView protein in InterPro
IPR012675 Beta-grasp_dom_sf
IPR010034 Mopterin_su_1
IPR016155 Mopterin_synth/thiamin_S_b
IPR003749 ThiS/MoaD-like
PfamiView protein in Pfam
PF02597 ThiS, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti9Q → E AA sequence (PubMed:8514782).Curated1
Sequence conflicti45A → R in CAA49864 (PubMed:8361352).Curated1

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
PATRICifig|1411691.4.peg.1494

Similar proteinsi

Entry informationi

Entry nameiMOAD_ECOLI
AccessioniPrimary (citable) accession number: P30748
Secondary accession number(s): P77422
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 164 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health