Q2YNT7 (MOAA_BRUA2) 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:	BAB1_0973

Organism

Brucella abortus (strain 2308) [Complete proteome] [HAMAP]

Taxonomic identifier

359391 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus

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_1000054175
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)
	Q2YNT7 [UniParc]. Last modified February 7, 2006. 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]

"Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM040264 Genomic DNA. Translation: CAJ10929.1.
RefSeq	YP_414393.1. NC_007618.1.
3D structure databases
HSSP	HSSP built from PDB template 2FB3 based on UniProtKB P69848.
ProteinModelPortal	Q2YNT7.
ModBase	Search...
Protein-protein interaction databases
STRING	359391.BAB1_0973.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ10929; CAJ10929; BAB1_0973.
GeneID	3787635.
KEGG	bmf:BAB1_0973.
PATRIC	17844877. VBIBruMel86222_1015.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2896.
HOGENOM	HOG000228680.
KO	K03639.
OMA	RNDHELV.
ProtClustDB	PRK00164.
Enzyme and pathway databases
BioCyc	BMEL359391:GJOQ-989-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_BRUA2

Accession

Primary (citable) accession number: Q2YNT7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 7, 2006
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program