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Protein

Molybdopterin-synthase adenylyltransferase

Gene

moeB

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

Functioni

Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD.2 Publications

Catalytic activityi

ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.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 sitei41 – 411ATP; via amide nitrogen
Binding sitei62 – 621ATP
Binding sitei86 – 861ATP
Metal bindingi172 – 1721Zinc
Metal bindingi175 – 1751Zinc
Metal bindingi244 – 2441Zinc
Metal bindingi247 – 2471Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi69 – 735ATP
Nucleotide bindingi130 – 1312ATP

GO - Molecular functioni

GO - Biological processi

  • cellular protein modification process Source: GO_Central
  • Mo-molybdopterin cofactor biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10154-MONOMER.
ECOL316407:JW0810-MONOMER.
MetaCyc:EG10154-MONOMER.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin-synthase adenylyltransferase (EC:2.7.7.80)
Alternative name(s):
MoaD protein adenylase
Molybdopterin-converting factor subunit 1 adenylase
Sulfur carrier protein MoaD adenylyltransferase
Gene namesi
Name:moeB
Synonyms:chlN
Ordered Locus Names:b0826, JW0810
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10154. moeB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141R → A or K: No effect. 1 Publication
Mutagenesisi14 – 141R → A: No activity; when associated with A-73. 1 Publication
Mutagenesisi44 – 441C → A: No effect. 1 Publication
Mutagenesisi73 – 731R → A: No effect. No activity; when associated with A-14. 1 Publication
Mutagenesisi73 – 731R → K: Substantially reduced activity. 1 Publication
Mutagenesisi128 – 1281C → A: No effect. 1 Publication
Mutagenesisi128 – 1281C → Y: No activity. 1 Publication
Mutagenesisi130 – 1301D → A: No activity. 1 Publication
Mutagenesisi130 – 1301D → E: Substantially reduced activity. 1 Publication
Mutagenesisi142 – 1421C → A: No effect. 1 Publication
Mutagenesisi172 – 1721C → A: No zinc bound and no enzyme activity. 1 Publication
Mutagenesisi175 – 1751C → A: No zinc bound and no enzyme activity. 1 Publication
Mutagenesisi187 – 1871C → A: No effect. 1 Publication
Mutagenesisi231 – 2311C → A: No effect. 1 Publication
Mutagenesisi244 – 2441C → A: No zinc bound and almost no enzyme activity. 1 Publication
Mutagenesisi247 – 2471C → A: No zinc bound and almost no enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Molybdopterin-synthase adenylyltransferasePRO_0000120575Add
BLAST

Proteomic databases

PaxDbiP12282.
PRIDEiP12282.

Interactioni

Subunit structurei

Homodimer. Forms a stable heterotetrameric complex of 2 MoeB and 2 MoaD during adenylation of MoaD.1 Publication

Protein-protein interaction databases

BioGridi4261831. 9 interactions.
DIPiDIP-10241N.
IntActiP12282. 15 interactions.
MINTiMINT-222244.
STRINGi511145.b0826.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 116Combined sources
Helixi13 – 164Combined sources
Turni19 – 213Combined sources
Helixi22 – 3110Combined sources
Beta strandi33 – 375Combined sources
Helixi41 – 5313Combined sources
Beta strandi56 – 616Combined sources
Helixi68 – 725Combined sources
Helixi79 – 813Combined sources
Helixi86 – 9712Combined sources
Beta strandi101 – 1066Combined sources
Helixi112 – 1209Combined sources
Beta strandi122 – 1276Combined sources
Helixi132 – 14514Combined sources
Beta strandi149 – 1568Combined sources
Beta strandi158 – 1647Combined sources
Helixi173 – 1775Combined sources
Helixi194 – 21320Combined sources
Beta strandi220 – 2278Combined sources
Turni228 – 2314Combined sources
Beta strandi232 – 2376Combined sources
Turni245 – 2473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JW9X-ray1.70B1-249[»]
1JWAX-ray2.90B1-249[»]
1JWBX-ray2.10B1-249[»]
ProteinModelPortaliP12282.
SMRiP12282. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12282.

Family & Domainsi

Sequence similaritiesi

Belongs to the HesA/MoeB/ThiF family.Curated

Phylogenomic databases

eggNOGiENOG4105D06. Bacteria.
COG0476. LUCA.
HOGENOMiHOG000281217.
InParanoidiP12282.
KOiK11996.
OMAiAGKIVMY.
OrthoDBiEOG628F8J.
PhylomeDBiP12282.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR012730. Mopterin_Synthase_Sase_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
TIGRFAMsiTIGR02355. moeB. 1 hit.

Sequencei

Sequence statusi: Complete.

P12282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELSDQEML RYNRQIILRG FDFDGQEALK DSRVLIVGLG GLGCAASQYL
60 70 80 90 100
ASAGVGNLTL LDFDTVSLSN LQRQTLHSDA TVGQPKVESA RDALTRINPH
110 120 130 140 150
IAITPVNALL DDAELAALIA EHDLVLDCTD NVAVRNQLNA GCFAAKVPLV
160 170 180 190 200
SGAAIRMEGQ ITVFTYQDGE PCYRCLSRLF GENALTCVEA GVMAPLIGVI
210 220 230 240
GSLQAMEAIK MLAGYGKPAS GKIVMYDAMT CQFREMKLMR NPGCEVCGQ
Length:249
Mass (Da):26,719
Last modified:October 1, 1989 - v1
Checksum:i12C77082B3F39D7D
GO

Mass spectrometryi

Molecular mass is 26563 Da from positions 1 - 249. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21151 Genomic DNA. Translation: AAA23580.1.
U00096 Genomic DNA. Translation: AAC73913.1.
AP009048 Genomic DNA. Translation: BAA35514.1.
PIRiB32352.
RefSeqiNP_415347.1. NC_000913.3.
WP_000829217.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73913; AAC73913; b0826.
BAA35514; BAA35514; BAA35514.
GeneIDi945452.
KEGGiecj:JW0810.
eco:b0826.
PATRICi32116855. VBIEscCol129921_0853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21151 Genomic DNA. Translation: AAA23580.1.
U00096 Genomic DNA. Translation: AAC73913.1.
AP009048 Genomic DNA. Translation: BAA35514.1.
PIRiB32352.
RefSeqiNP_415347.1. NC_000913.3.
WP_000829217.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JW9X-ray1.70B1-249[»]
1JWAX-ray2.90B1-249[»]
1JWBX-ray2.10B1-249[»]
ProteinModelPortaliP12282.
SMRiP12282. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261831. 9 interactions.
DIPiDIP-10241N.
IntActiP12282. 15 interactions.
MINTiMINT-222244.
STRINGi511145.b0826.

Proteomic databases

PaxDbiP12282.
PRIDEiP12282.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73913; AAC73913; b0826.
BAA35514; BAA35514; BAA35514.
GeneIDi945452.
KEGGiecj:JW0810.
eco:b0826.
PATRICi32116855. VBIEscCol129921_0853.

Organism-specific databases

EchoBASEiEB0152.
EcoGeneiEG10154. moeB.

Phylogenomic databases

eggNOGiENOG4105D06. Bacteria.
COG0476. LUCA.
HOGENOMiHOG000281217.
InParanoidiP12282.
KOiK11996.
OMAiAGKIVMY.
OrthoDBiEOG628F8J.
PhylomeDBiP12282.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:EG10154-MONOMER.
ECOL316407:JW0810-MONOMER.
MetaCyc:EG10154-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP12282.
PROiP12282.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR012730. Mopterin_Synthase_Sase_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
TIGRFAMsiTIGR02355. moeB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis."
    Nohno T., Kasai Y., Saito T.
    J. Bacteriol. 170:4097-4102(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ZK126.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli."
    Leimkuehler S., Rajagopalan K.V.
    J. Biol. Chem. 276:22024-22031(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SULFUR DONOR.
  6. "Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor."
    Leimkuehler S., Wuebbens M.M., Rajagopalan K.V.
    J. Biol. Chem. 276:34695-34701(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, INTERACTION WITH MOAD, MUTAGENESIS OF CYS-44; CYS-128; CYS-142; CYS-172; CYS-175; CYS-187; CYS-231; CYS-244 AND CYS-247, MASS SPECTROMETRY.
    Strain: K12 / DH5-alpha.
  7. "Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex."
    Lake M.W., Wuebbens M.M., Rajagopalan K.V., Schindelin H.
    Nature 414:325-329(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH MOAD; ZINC; MOAD AND ATP AND MOAD-ADENYLATE, MUTAGENESIS OF ARG-14; ARG-73 AND ASP-130, REACTION MECHANISM.

Entry informationi

Entry nameiMOEB_ECOLI
AccessioniPrimary (citable) accession number: P12282
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 17, 2016
This is version 142 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, 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.