Reviewed, UniProtKB/Swiss-Prot P12039 (PUR2_BACSU)

Names and origin

Protein names

Recommended name:
    Phosphoribosylamine--glycine ligase
    EC=6.3.4.13
Alternative name(s):
    GARS
    Glycinamide ribonucleotide synthetase
    Phosphoribosylglycinamide synthetase

Gene names

Name:	purD
Ordered Locus Names:	BSU06530

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. HAMAP MF_00138
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. HAMAP MF_00138
Sequence similarities	Belongs to the GARS family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine base biosynthetic process Inferred from electronic annotation. Source: InterPro purine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosylamine-glycine ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 422	422	Phosphoribosylamine--glycine ligase HAMAP MF_00138		PRO_0000151436
Regions
	Domain	107 – 313	207	ATP-grasp
	Nucleotide binding	133 – 194	62	ATP By similarity
Sites
	Metal binding	283	1	Magnesium or manganese By similarity
	Metal binding	285	1	Magnesium or manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12039-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 4EF390A85CC90FB2	FASTA	422	45,280
	10 20 30 40 50 60 MNVLIIGKGG REHTLAWKAA QSSLVENVFA APGNDGMAAS AQLVNIEESD HAGLVSFAKQ 70 80 90 100 110 120 NQVGLTIVGP EVPLIEGLVD EFEKAGLHVF GPSKAAAIIE GSKQFAKDLM KKYDIPTAEY 130 140 150 160 170 180 ETFTSFDEAK AYVQEKGAPI VIKADGLAAG KGVTVAMTEE EAIACLHDFL EDEKFGDASA 190 200 210 220 230 240 SVVIEEYLSG EEFSLMAFVK GEKVYPMVIA QDHKRAFDGD KGPNTGGMGA YSPVPQISEE 250 260 270 280 290 300 TVRHAVETIV KPAAKAMVQE GRSFTGVLYA GLMLTENGSK VIEFNARFGD PETQVVLPRM 310 320 330 340 350 360 ESDLVQVLLD LLDDKEVDLR WKDTAAVSVV LASEGYPESY AKGTPIGSLA AETEQVVVFH 370 380 390 400 410 420 AGTKAEGGEF VTNGGRVANV TAFDETFEAA RDRVYKAVDE IFKPGLFFRK DIGARALKAA QK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis." Ebbole D.J., Zalkin H. J. Biol. Chem. 262:8274-8287(1987) [PubMed: 3036807] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a region devoted to purine uptake and metabolism, and containing the genes cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide sequence." Borriss R., Porwollik S., Schroeter R. Microbiology 142:3027-3031(1996) [PubMed: 8969499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02732 Genomic DNA. Translation: AAA22684.1. AF011544 Genomic DNA. Translation: AAB72186.1. AL009126 Genomic DNA. Translation: CAB12473.1.
PIR	AJBSAG. B29183.
RefSeq	NP_388535.1.
3D structure databases
HSSP	HSSP built from PDB template 1GSO based on UniProtKB P15640.
ModBase	Search...
Genome annotation databases
GeneID	938741.
GenomeReviews	Gene locus BSU06530 in contig AL009126_GR.
KEGG	bsu:BSU06530.
NMPDR	fig|224308.1.peg.654.
Organism-specific databases
SubtiList	BG10711. purD. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P12039.
OMA	IEYNCRF.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU0654-MON.
BRENDA	6.3.4.13. 150.
Family and domain databases
HAMAP	MF_00138. [Tree]
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR013817. Pre-ATP_grasp. IPR020561. PRibGlycinamid_synth_ATP-grasp. IPR000115. PRibGlycinamide_synth. IPR020560. PRibGlycinamide_synth_C-dom. IPR020559. PRibGlycinamide_synth_CS. IPR020562. PRibGlycinamide_synth_N-dom. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF01071. GARS_A. 1 hit. PF02843. GARS_C. 1 hit. PF02844. GARS_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00877. purD. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00184. GARS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR2_BACSU

Accession

Primary (citable) accession number: P12039

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 3, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)