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Protein

Cyclic pyranopterin monophosphate synthase accessory protein

Gene

moaC

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

Functioni

Together with MoaA, is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).

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
Active sitei128 – 1281Sequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11666-MONOMER.
ECOL316407:JW0766-MONOMER.
MetaCyc:EG11666-MONOMER.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic pyranopterin monophosphate synthase accessory protein
Alternative name(s):
Molybdenum cofactor biosynthesis protein C
Gene namesi
Name:moaC
Synonyms:chlA3
Ordered Locus Names:b0783, JW0766
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11666. moaC.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511K → A: Reduced activity. 1 Publication
Mutagenesisi52 – 521G → A: Reduced activity. 1 Publication
Mutagenesisi67 – 671K → A: Reduced activity. 1 Publication
Mutagenesisi76 – 761C → A: Reduced activity. 1 Publication
Mutagenesisi77 – 771H → A: Reduced activity. 1 Publication
Mutagenesisi110 – 1101G → A: Reduced activity. 1 Publication
Mutagenesisi112 – 1121E → A: Reduced activity. 1 Publication
Mutagenesisi117 – 1171T → P: Strongly reduced activity. 1 Publication
Mutagenesisi128 – 1281D → A: Loss of activity. 1 Publication
Mutagenesisi131 – 1311K → A: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 161160Cyclic pyranopterin monophosphate synthase accessory proteinPRO_0000097798Add
BLAST

Proteomic databases

EPDiP0A738.
PaxDbiP0A738.

Expressioni

Inductioni

By anaerobiosis, repressed by the molybdenum cofactor.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi4262176. 8 interactions.
DIPiDIP-10230N.
IntActiP0A738. 20 interactions.
MINTiMINT-1231800.
STRINGi511145.b0783.

Structurei

Secondary structure

1
161
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 213Combined sources
Beta strandi24 – 3512Combined sources
Helixi38 – 469Combined sources
Turni47 – 493Combined sources
Beta strandi50 – 523Combined sources
Helixi54 – 6714Combined sources
Helixi69 – 724Combined sources
Beta strandi82 – 9110Combined sources
Helixi92 – 943Combined sources
Beta strandi96 – 10914Combined sources
Helixi112 – 13019Combined sources
Turni131 – 1333Combined sources
Beta strandi138 – 1458Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKRX-ray2.00A1-161[»]
1EKSX-ray2.50A1-161[»]
4PYAX-ray1.79A3-161[»]
4PYDX-ray3.19A/B/C/D/E/F1-161[»]
ProteinModelPortaliP0A738.
SMRiP0A738. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A738.

Family & Domainsi

Sequence similaritiesi

Belongs to the MoaC family.Curated

Phylogenomic databases

eggNOGiENOG4108YXW. Bacteria.
COG0315. LUCA.
HOGENOMiHOG000228417.
InParanoidiP0A738.
KOiK03637.
OMAiTTFTHIN.
OrthoDBiEOG6SV58B.
PhylomeDBiP0A738.

Family and domain databases

Gene3Di3.30.70.640. 1 hit.
HAMAPiMF_01224_B. MoaC_B.
InterProiIPR023045. Mo_CF_biosynth-C.
IPR023046. Mo_CF_biosynth-C_bac.
IPR002820. Mopterin_CF_biosynth-C_dom.
[Graphical view]
PfamiPF01967. MoaC. 1 hit.
[Graphical view]
SUPFAMiSSF55040. SSF55040. 1 hit.
TIGRFAMsiTIGR00581. moaC. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0A738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLTHINAA GEAHMVDVSA KAETVREARA EAFVTMRSET LAMIIDGRHH
60 70 80 90 100
KGDVFATARI AGIQAAKRTW DLIPLCHPLM LSKVEVNLQA EPEHNRVRIE
110 120 130 140 150
TLCRLTGKTG VEMEALTAAS VAALTIYDMC KAVQKDMVIG PVRLLAKSGG
160
KSGDFKVEAD D
Length:161
Mass (Da):17,467
Last modified:January 23, 2007 - v2
Checksum:i280DAC1EFAAA04AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171D → N in CAA49863 (PubMed:8361352).Curated
Sequence conflicti92 – 976PEHNRV → RAQSG in CAA49863 (PubMed:8361352).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49863.1.
U00096 Genomic DNA. Translation: AAC73870.1.
AP009048 Genomic DNA. Translation: BAA35441.1.
PIRiG64814.
RefSeqiNP_415304.1. NC_000913.3.
WP_000080885.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73870; AAC73870; b0783.
BAA35441; BAA35441; BAA35441.
GeneIDi945397.
KEGGiecj:JW0766.
eco:b0783.
PATRICi32116767. VBIEscCol129921_0809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49863.1.
U00096 Genomic DNA. Translation: AAC73870.1.
AP009048 Genomic DNA. Translation: BAA35441.1.
PIRiG64814.
RefSeqiNP_415304.1. NC_000913.3.
WP_000080885.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKRX-ray2.00A1-161[»]
1EKSX-ray2.50A1-161[»]
4PYAX-ray1.79A3-161[»]
4PYDX-ray3.19A/B/C/D/E/F1-161[»]
ProteinModelPortaliP0A738.
SMRiP0A738. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262176. 8 interactions.
DIPiDIP-10230N.
IntActiP0A738. 20 interactions.
MINTiMINT-1231800.
STRINGi511145.b0783.

Proteomic databases

EPDiP0A738.
PaxDbiP0A738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73870; AAC73870; b0783.
BAA35441; BAA35441; BAA35441.
GeneIDi945397.
KEGGiecj:JW0766.
eco:b0783.
PATRICi32116767. VBIEscCol129921_0809.

Organism-specific databases

EchoBASEiEB1617.
EcoGeneiEG11666. moaC.

Phylogenomic databases

eggNOGiENOG4108YXW. Bacteria.
COG0315. LUCA.
HOGENOMiHOG000228417.
InParanoidiP0A738.
KOiK03637.
OMAiTTFTHIN.
OrthoDBiEOG6SV58B.
PhylomeDBiP0A738.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:EG11666-MONOMER.
ECOL316407:JW0766-MONOMER.
MetaCyc:EG11666-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A738.
PROiP0A738.

Family and domain databases

Gene3Di3.30.70.640. 1 hit.
HAMAPiMF_01224_B. MoaC_B.
InterProiIPR023045. Mo_CF_biosynth-C.
IPR023046. Mo_CF_biosynth-C_bac.
IPR002820. Mopterin_CF_biosynth-C_dom.
[Graphical view]
PfamiPF01967. MoaC. 1 hit.
[Graphical view]
SUPFAMiSSF55040. SSF55040. 1 hit.
TIGRFAMsiTIGR00581. moaC. 1 hit.
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. "Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC."
    Wuebbens M.M., Liu M.T.W., Rajagopalan K.V., Schindelin H.
    Structure 8:709-718(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF LYS-51; GLY-52; LYS-67; CYS-76; HIS-77; GLY-110; GLU-112; THR-117; ASP-128 AND LYS-131.

Entry informationi

Entry nameiMOAC_ECOLI
AccessioniPrimary (citable) accession number: P0A738
Secondary accession number(s): P30747, P77530
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 101 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.