Q57DG3 (MOAA_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclic pyranopterin monophosphate synthase
EC=4.1.99.18

Alternative name(s):
Molybdenum cofactor biosynthesis protein A

Gene names

Name:	moaA
Ordered Locus Names:	BruAb1_0964

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus › Brucella abortus bv. 1

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z) By similarity. HAMAP-Rule MF_01225
Catalytic activity	GTP = cyclic pyranopterin monophosphate + diphosphate. HAMAP-Rule MF_01225
Cofactor	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.
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis. HAMAP-Rule MF_01225
Subunit structure	Monomer and homodimer By similarity.
Sequence similarities	Belongs to the radical SAM superfamily. MoaA family.

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Ligand	4Fe-4S GTP-binding Iron Iron-sulfur Metal-binding Nucleotide-binding S-adenosyl-L-methionine
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	molybdopterin synthase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW lyase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	Cyclic pyranopterin monophosphate synthase HAMAP-Rule MF_01225		PRO_1000054176
Regions
	Region	273 – 275	3	GTP binding By similarity
Sites
	Metal binding	35	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	39	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	42	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	268	1	Iron-sulfur 2 (4Fe-4S-substrate) By similarity
	Metal binding	271	1	Iron-sulfur 2 (4Fe-4S-substrate) By similarity
	Metal binding	285	1	Iron-sulfur 2 (4Fe-4S-substrate) By similarity
	Binding site	28	1	GTP By similarity
	Binding site	41	1	S-adenosyl-L-methionine By similarity
	Binding site	77	1	GTP By similarity
	Binding site	81	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	111	1	GTP By similarity
	Binding site	135	1	S-adenosyl-L-methionine By similarity
	Binding site	171	1	GTP By similarity
	Binding site	205	1	S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57DG3 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 50B8258570E51148	FASTA	344	38,687
	10 20 30 40 50 60 MRNVQDQPLV SPTEPMIDPF GRAVTYLRVS VTDRCDFRCT YCMAEHMTFL PKKDLLTLEE 70 80 90 100 110 120 LDRLCSVFIE KGVRKLRLTG GEPLVRKNIM HLIGNLSRHL KSGALDELTL TTNGSQLARF 130 140 150 160 170 180 AGELADCGVR RINVSLDTLN PEKFRTITRW GDLSRVLEGI DAAQKAAIHV KINAVALKDF 190 200 210 220 230 240 NDAEIPELIR WAHGRGMDVT LIETMPMGEI EFDRTDQYLP LSQVRADLAS QFTLADIPYR 250 260 270 280 290 300 TGGPARYVTI SETGGRLGFI TPMTYNFCES CNRVRLTCTG MLYMCLGQND DADLRKALRE 310 320 330 340 SESDEHLSQA IDEAISRKPK GHDFIIDREH NRPSVARHMS LTGG

References

[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(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX74321.1.
RefSeq	YP_221682.1. NC_006932.1.
3D structure databases
HSSP	HSSP built from PDB template 1TV8 based on UniProtKB P65388.
ProteinModelPortal	Q57DG3.
ModBase	Search...
Protein-protein interaction databases
STRING	262698.BruAb1_0964.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX74321; AAX74321; BruAb1_0964.
GeneID	3340016.
KEGG	bmb:BruAb1_0964.
PATRIC	17823572. VBIBruAbo15061_1015.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2896.
HOGENOM	HOG000228680.
KO	K03639.
OMA	RNDHELV.
ProtClustDB	PRK00164.
Enzyme and pathway databases
BioCyc	BABO262698:GJC2-979-MONOMER.
UniPathway	UPA00344.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01225_B. MoaA_B.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR013483. MoaA. IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS. IPR010505. Mob_synth_C. IPR007197. rSAM. [Graphical view]
Pfam	PF06463. Mob_synth_C. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR02666. moaA. 1 hit.
PROSITE	PS01305. MOAA_NIFB_PQQE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MOAA_BRUAB

Accession

Primary (citable) accession number: Q57DG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program