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Protein

Cyclic pyranopterin monophosphate synthase

Gene

moaA

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

Functioni

Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).

Catalytic activityi

GTP = cyclic pyranopterin phosphate + diphosphate.

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.By similarity
  • S-adenosyl-L-methionineBy similarityNote: Binds 1 S-adenosyl-L-methionine per subunit.By similarity

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 sitei17 – 171GTPBy similarity
Metal bindingi24 – 241Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Metal bindingi28 – 281Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Binding sitei30 – 301S-adenosyl-L-methionineBy similarity
Metal bindingi31 – 311Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Binding sitei68 – 681GTPBy similarity
Binding sitei72 – 721S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei99 – 991GTPBy similarity
Binding sitei123 – 1231S-adenosyl-L-methionineBy similarity
Binding sitei160 – 1601GTPBy similarity
Binding sitei194 – 1941S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi257 – 2571Iron-sulfur 2 (4Fe-4S-substrate)By similarity
Metal bindingi260 – 2601Iron-sulfur 2 (4Fe-4S-substrate)By similarity
Metal bindingi274 – 2741Iron-sulfur 2 (4Fe-4S-substrate)By similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • cyclic pyranopterin monophosphate synthase activity Source: EcoCyc
  • GTP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • molybdopterin cofactor biosynthetic process Source: EcoCyc
  • Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
  • response to heat Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

4Fe-4S, GTP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:EG11595-MONOMER.
ECOL316407:JW0764-MONOMER.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic pyranopterin monophosphate synthase (EC:4.1.99.18)
Alternative name(s):
Molybdenum cofactor biosynthesis protein A
Gene namesi
Name:moaA
Synonyms:bisA, chlA, chlA1, narA
Ordered Locus Names:b0781, JW0764
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11595. moaA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Cyclic pyranopterin monophosphate synthasePRO_0000152958Add
BLAST

Proteomic databases

PaxDbiP30745.
PRIDEiP30745.

Expressioni

Inductioni

By anaerobiosis, repressed by the molybdenum cofactor.

Interactioni

Subunit structurei

Monomer and homodimer.By similarity

Protein-protein interaction databases

BioGridi4259951. 5 interactions.
DIPiDIP-10228N.
IntActiP30745. 13 interactions.
MINTiMINT-1229909.
STRINGi511145.b0781.

Structurei

3D structure databases

ProteinModelPortaliP30745.
SMRiP30745. Positions 4-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni262 – 2643GTP bindingBy similarity

Sequence similaritiesi

Belongs to the radical SAM superfamily. MoaA family.Curated

Phylogenomic databases

eggNOGiENOG4105CM1. Bacteria.
COG2896. LUCA.
HOGENOMiHOG000228682.
InParanoidiP30745.
KOiK03639.
OMAiGWIHQIR.
OrthoDBiEOG64XXNN.
PhylomeDBiP30745.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01225_B. MoaA_B.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR013483. MoaA.
IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS.
IPR010505. Mob_synth_C.
IPR007197. rSAM.
[Graphical view]
PfamiPF06463. Mob_synth_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02666. moaA. 1 hit.
PROSITEiPS01305. MOAA_NIFB_PQQE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQLTDAFA RKFYYLRLSI TDVCNFRCTY CLPDGYKPSG VTNKGFLTVD
60 70 80 90 100
EIRRVTRAFA RLGTEKVRLT GGEPSLRRDF TDIIAAVREN DAIRQIAVTT
110 120 130 140 150
NGYRLERDVA SWRDAGLTGI NVSVDSLDAR QFHAITGQDK FNQVMAGIDA
160 170 180 190 200
AFEAGFEKVK VNTVLMRDVN HHQLDTFLNW IQHRPIQLRF IELMETGEGS
210 220 230 240 250
ELFRKHHISG QVLRDELLRR GWIHQLRQRS DGPAQVFCHP DYAGEIGLIM
260 270 280 290 300
PYEKDFCATC NRLRVSSIGK LHLCLFGEGG VNLRDLLEDD TQQQALEARI
310 320
SAALREKKQT HFLHQNNTGI TQNLSYIGG
Length:329
Mass (Da):37,346
Last modified:April 1, 1993 - v1
Checksum:iFE91263C53F33F78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49861.1.
U00096 Genomic DNA. Translation: AAC73868.1.
AP009048 Genomic DNA. Translation: BAA35439.1.
PIRiS31879.
RefSeqiNP_415302.1. NC_000913.3.
WP_001350494.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73868; AAC73868; b0781.
BAA35439; BAA35439; BAA35439.
GeneIDi945392.
KEGGiecj:JW0764.
eco:b0781.
PATRICi32116763. VBIEscCol129921_0807.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49861.1.
U00096 Genomic DNA. Translation: AAC73868.1.
AP009048 Genomic DNA. Translation: BAA35439.1.
PIRiS31879.
RefSeqiNP_415302.1. NC_000913.3.
WP_001350494.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP30745.
SMRiP30745. Positions 4-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259951. 5 interactions.
DIPiDIP-10228N.
IntActiP30745. 13 interactions.
MINTiMINT-1229909.
STRINGi511145.b0781.

Proteomic databases

PaxDbiP30745.
PRIDEiP30745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73868; AAC73868; b0781.
BAA35439; BAA35439; BAA35439.
GeneIDi945392.
KEGGiecj:JW0764.
eco:b0781.
PATRICi32116763. VBIEscCol129921_0807.

Organism-specific databases

EchoBASEiEB1552.
EcoGeneiEG11595. moaA.

Phylogenomic databases

eggNOGiENOG4105CM1. Bacteria.
COG2896. LUCA.
HOGENOMiHOG000228682.
InParanoidiP30745.
KOiK03639.
OMAiGWIHQIR.
OrthoDBiEOG64XXNN.
PhylomeDBiP30745.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:EG11595-MONOMER.
ECOL316407:JW0764-MONOMER.

Miscellaneous databases

PROiP30745.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01225_B. MoaA_B.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR013483. MoaA.
IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS.
IPR010505. Mob_synth_C.
IPR007197. rSAM.
[Graphical view]
PfamiPF06463. Mob_synth_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02666. moaA. 1 hit.
PROSITEiPS01305. MOAA_NIFB_PQQE. 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 1-10.
    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.

Entry informationi

Entry nameiMOAA_ECOLI
AccessioniPrimary (citable) accession number: P30745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: February 17, 2016
This is version 137 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

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. 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.