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Protein

Cyclic pyranopterin monophosphate synthase

Gene

moaA

Organism
Brucella abortus biovar 1 (strain 9-941)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

GTP = cyclic pyranopterin phosphate + diphosphate.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: 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.UniRule annotation
  • S-adenosyl-L-methionineUniRule annotationNote: Binds 1 S-adenosyl-L-methionine per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281GTPUniRule annotation
Metal bindingi35 – 351Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi39 – 391Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Binding sitei41 – 411S-adenosyl-L-methionineUniRule annotation
Metal bindingi42 – 421Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Binding sitei77 – 771GTPUniRule annotation
Binding sitei81 – 811S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
Binding sitei111 – 1111GTPUniRule annotation
Binding sitei135 – 1351S-adenosyl-L-methionineUniRule annotation
Binding sitei171 – 1711GTPUniRule annotation
Binding sitei205 – 2051S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation
Metal bindingi268 – 2681Iron-sulfur 2 (4Fe-4S-substrate)UniRule annotation
Metal bindingi271 – 2711Iron-sulfur 2 (4Fe-4S-substrate)UniRule annotation
Metal bindingi285 – 2851Iron-sulfur 2 (4Fe-4S-substrate)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. cyclic pyranopterin monophosphate synthase activity Source: UniProtKB-EC
  3. GTP binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciBABO262698:GJC2-979-MONOMER.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic pyranopterin monophosphate synthaseUniRule annotation (EC:4.1.99.18UniRule annotation)
Alternative name(s):
Molybdenum cofactor biosynthesis protein AUniRule annotation
Gene namesi
Name:moaAUniRule annotation
Ordered Locus Names:BruAb1_0964
OrganismiBrucella abortus biovar 1 (strain 9-941)
Taxonomic identifieri262698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000540 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. molybdopterin synthase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Cyclic pyranopterin monophosphate synthasePRO_1000054176Add
BLAST

Interactioni

Subunit structurei

Monomer and homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi262698.BruAb1_0964.

Structurei

3D structure databases

ProteinModelPortaliQ57DG3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni273 – 2753GTP bindingUniRule annotation

Sequence similaritiesi

Belongs to the radical SAM superfamily. MoaA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2896.
HOGENOMiHOG000228680.
KOiK03639.
OMAiTREMHDR.
OrthoDBiEOG64XXNN.

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.

Q57DG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNVQDQPLV SPTEPMIDPF GRAVTYLRVS VTDRCDFRCT YCMAEHMTFL
60 70 80 90 100
PKKDLLTLEE LDRLCSVFIE KGVRKLRLTG GEPLVRKNIM HLIGNLSRHL
110 120 130 140 150
KSGALDELTL TTNGSQLARF AGELADCGVR RINVSLDTLN PEKFRTITRW
160 170 180 190 200
GDLSRVLEGI DAAQKAAIHV KINAVALKDF NDAEIPELIR WAHGRGMDVT
210 220 230 240 250
LIETMPMGEI EFDRTDQYLP LSQVRADLAS QFTLADIPYR TGGPARYVTI
260 270 280 290 300
SETGGRLGFI TPMTYNFCES CNRVRLTCTG MLYMCLGQND DADLRKALRE
310 320 330 340
SESDEHLSQA IDEAISRKPK GHDFIIDREH NRPSVARHMS LTGG
Length:344
Mass (Da):38,687
Last modified:May 10, 2005 - v1
Checksum:i50B8258570E51148
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017223 Genomic DNA. Translation: AAX74321.1.
RefSeqiYP_221682.1. NC_006932.1.

Genome annotation databases

EnsemblBacteriaiAAX74321; AAX74321; BruAb1_0964.
KEGGibmb:BruAb1_0964.
PATRICi17823572. VBIBruAbo15061_1015.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017223 Genomic DNA. Translation: AAX74321.1.
RefSeqiYP_221682.1. NC_006932.1.

3D structure databases

ProteinModelPortaliQ57DG3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262698.BruAb1_0964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAX74321; AAX74321; BruAb1_0964.
KEGGibmb:BruAb1_0964.
PATRICi17823572. VBIBruAbo15061_1015.

Phylogenomic databases

eggNOGiCOG2896.
HOGENOMiHOG000228680.
KOiK03639.
OMAiTREMHDR.
OrthoDBiEOG64XXNN.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciBABO262698:GJC2-979-MONOMER.

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

  1. "Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
    Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
    J. Bacteriol. 187:2715-2726(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 9-941.

Entry informationi

Entry nameiMOAA_BRUAB
AccessioniPrimary (citable) accession number: Q57DG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 10, 2005
Last modified: April 1, 2015
This is version 68 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

Documents

  1. Brucella abortus strain 9-941
    Brucella abortus (strain 9-941): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.