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Protein

Molybdenum cofactor biosynthesis protein B

Gene

moaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the biosynthesis of molybdopterin. Can bind GTP and has low GTPase activity. Can bind MPT, but has no MPT adenylyl transferase activity.

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 sitei110 – 1101GTPCurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-1501.
ECOL316407:JW0765-MONOMER.
RETL1328306-WGS:GSTH-886-MONOMER.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdenum cofactor biosynthesis protein B
Gene namesi
Name:moaB
Synonyms:chlA2
Ordered Locus Names:b0782, JW0765
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11596. moaB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 170169Molybdenum cofactor biosynthesis protein BPRO_0000170970Add
BLAST

Proteomic databases

EPDiP0AEZ9.
PaxDbiP0AEZ9.
PRIDEiP0AEZ9.

2D gel databases

SWISS-2DPAGEP0AEZ9.

Expressioni

Inductioni

By anaerobiosis, repressed by the molybdenum cofactor.

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259950. 14 interactions.
IntActiP0AEZ9. 4 interactions.
MINTiMINT-1301713.
STRINGi511145.b0782.

Structurei

Secondary structure

1
170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187Combined sources
Helixi24 – 263Combined sources
Helixi28 – 3912Combined sources
Beta strandi43 – 508Combined sources
Helixi54 – 6613Combined sources
Beta strandi67 – 693Combined sources
Beta strandi72 – 776Combined sources
Beta strandi80 – 823Combined sources
Helixi87 – 915Combined sources
Helixi92 – 943Combined sources
Beta strandi96 – 983Combined sources
Helixi100 – 11415Combined sources
Helixi115 – 1206Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi131 – 1366Combined sources
Helixi140 – 14910Combined sources
Helixi151 – 1555Combined sources
Helixi165 – 1673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKZX-ray1.60A/B1-170[»]
1R2KX-ray2.10A/B2-170[»]
ProteinModelPortaliP0AEZ9.
SMRiP0AEZ9. Positions 3-170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEZ9.

Family & Domainsi

Sequence similaritiesi

Belongs to the MoaB/Mog family.Curated

Phylogenomic databases

eggNOGiENOG4108RIR. Bacteria.
COG0521. LUCA.
HOGENOMiHOG000281102.
InParanoidiP0AEZ9.
KOiK03638.
OMAiIGTATIQ.
OrthoDBiEOG60PHHC.
PhylomeDBiP0AEZ9.

Family and domain databases

Gene3Di3.40.980.10. 1 hit.
InterProiIPR012245. MoaB.
IPR001453. MoaB/Mog_dom.
IPR013484. MoaB_proteobac.
IPR008284. MoCF_biosynth_CS.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
[Graphical view]
PIRSFiPIRSF006443. MoaB. 1 hit.
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.
TIGRFAMsiTIGR02667. moaB_proteo. 1 hit.
TIGR00177. molyb_syn. 1 hit.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVSTEFIP TRIAILTVSN RRGEEDDTSG HYLRDSAQEA GHHVVDKAIV
60 70 80 90 100
KENRYAIRAQ VSAWIASDDV QVVLITGGTG LTEGDQAPEA LLPLFDREVE
110 120 130 140 150
GFGEVFRMLS FEEIGTSTLQ SRAVAGVANK TLIFAMPGST KACRTAWENI
160 170
IAPQLDARTR PCNFHPHLKK
Length:170
Mass (Da):18,665
Last modified:January 23, 2007 - v2
Checksum:iC9AA21A7E12E53B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49862.1.
U00096 Genomic DNA. Translation: AAC73869.1.
AP009048 Genomic DNA. Translation: BAA35440.1.
PIRiS34999. S31880.
RefSeqiNP_415303.1. NC_000913.3.
WP_000084639.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73869; AAC73869; b0782.
BAA35440; BAA35440; BAA35440.
GeneIDi945396.
KEGGiecj:JW0765.
eco:b0782.
PATRICi32116765. VBIEscCol129921_0808.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49862.1.
U00096 Genomic DNA. Translation: AAC73869.1.
AP009048 Genomic DNA. Translation: BAA35440.1.
PIRiS34999. S31880.
RefSeqiNP_415303.1. NC_000913.3.
WP_000084639.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MKZX-ray1.60A/B1-170[»]
1R2KX-ray2.10A/B2-170[»]
ProteinModelPortaliP0AEZ9.
SMRiP0AEZ9. Positions 3-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259950. 14 interactions.
IntActiP0AEZ9. 4 interactions.
MINTiMINT-1301713.
STRINGi511145.b0782.

2D gel databases

SWISS-2DPAGEP0AEZ9.

Proteomic databases

EPDiP0AEZ9.
PaxDbiP0AEZ9.
PRIDEiP0AEZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73869; AAC73869; b0782.
BAA35440; BAA35440; BAA35440.
GeneIDi945396.
KEGGiecj:JW0765.
eco:b0782.
PATRICi32116765. VBIEscCol129921_0808.

Organism-specific databases

EchoBASEiEB1553.
EcoGeneiEG11596. moaB.

Phylogenomic databases

eggNOGiENOG4108RIR. Bacteria.
COG0521. LUCA.
HOGENOMiHOG000281102.
InParanoidiP0AEZ9.
KOiK03638.
OMAiIGTATIQ.
OrthoDBiEOG60PHHC.
PhylomeDBiP0AEZ9.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:MONOMER0-1501.
ECOL316407:JW0765-MONOMER.
RETL1328306-WGS:GSTH-886-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AEZ9.
PROiP0AEZ9.

Family and domain databases

Gene3Di3.40.980.10. 1 hit.
InterProiIPR012245. MoaB.
IPR001453. MoaB/Mog_dom.
IPR013484. MoaB_proteobac.
IPR008284. MoCF_biosynth_CS.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
[Graphical view]
PIRSFiPIRSF006443. MoaB. 1 hit.
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.
TIGRFAMsiTIGR02667. moaB_proteo. 1 hit.
TIGR00177. molyb_syn. 1 hit.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis."
    Rivers S.L., McNairn E., Blasco F., Giordano G., Boxer D.H.
    Mol. Microbiol. 8:1071-1081(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  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. "Function of MoaB proteins in the biosynthesis of the molybdenum and tungsten cofactors."
    Bevers L.E., Hagedoorn P.L., Santamaria-Araujo J.A., Magalon A., Hagen W.R., Schwarz G.
    Biochemistry 47:949-956(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING OF MPT, LACK OF FUNCTION AS MPT ADENYLYLTRANSFERASE.
  6. "Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli."
    Bader G., Gomez-Ortiz M., Haussmann C., Bacher A., Huber R., Fischer M.
    Acta Crystallogr. D 60:1068-1075(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  7. "The crystal structure of Escherichia coli MoaB suggests a probable role in molybdenum cofactor synthesis."
    Sanishvili R., Beasley S., Skarina T., Glesne D., Joachimiak A., Edwards A., Savchenko A.
    J. Biol. Chem. 279:42139-42146(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), GTP BINDING, SUBUNIT.

Entry informationi

Entry nameiMOAB_ECOLI
AccessioniPrimary (citable) accession number: P0AEZ9
Secondary accession number(s): P30746
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 91 of the entry and version 2 of the sequence. [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

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.