A1KP87 (GUAA_MYCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GMP synthase [glutamine-hydrolyzing]
EC=6.3.5.2

Alternative name(s):
GMP synthetase
Glutamine amidotransferase

Gene names

Name:	guaA
Ordered Locus Names:	BCG_3466c

Organism

Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]

Taxonomic identifier

410289 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis › Mycobacterium bovis BCG

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the synthesis of GMP from XMP By similarity.
Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP-Rule MF_00344
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP-Rule MF_00344
Subunit structure	Homodimer By similarity.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain. Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	GMP biosynthetic process Inferred from electronic annotation. Source: HAMAP glutamine metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP GMP synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP pyrophosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 525	525	GMP synthase [glutamine-hydrolyzing] HAMAP-Rule MF_00344		PRO_1000120337
Regions
	Domain	16 – 205	190	Glutamine amidotransferase type-1
	Domain	206 – 399	194	GMPS ATP-PPase
	Nucleotide binding	233 – 239	7	ATP By similarity
Sites
	Active site	93	1	Nucleophile By similarity
	Active site	179	1	By similarity
	Active site	181	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1KP87 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: DFBE06100BA16FAF	FASTA	525	56,060
	10 20 30 40 50 60 MVQPADIDVP ETPARPVLVV DFGAQYAQLI ARRVREARVF SEVIPHTASI EEIRARQPVA 70 80 90 100 110 120 LVLSGGPASV YADGAPKLDP ALLDLGVPVL GICYGFQAMA QALGGIVAHT GTREYGRTEL 130 140 150 160 170 180 KVLGGKLHSD LPEVQPVWMS HGDAVTAAPD GFDVVASSAG APVAAFEAFD RRLAGVQYHP 190 200 210 220 230 240 EVMHTPHGQQ VLSRFLHDFA GLGAQWTPAN IANALIEQVR TQIGDGHAIC GLSGGVDSAV 250 260 270 280 290 300 AAALVQRAIG DRLTCVFVDH GLLRAGERAQ VQRDFVAATG ANLVTVDAAE TFLEALSGVS 310 320 330 340 350 360 APEGKRKIIG RQFIRAFEGA VRDVLDGKTA EFLVQGTLYP DVVESGGGSG TANIKSHHNV 370 380 390 400 410 420 GGLPDDLKFT LVEPLRLLFK DEVRAVGREL GLPEEIVARQ PFPGPGLGIR IVGEVTAKRL 430 440 450 460 470 480 DTLRHADSIV REELTAAGLD NQIWQCPVVL LADVRSVGVQ GDGRTYGHPI VLRPVSSEDA 490 500 510 520 MTADWTRVPY EVLERISTRI TNEVAEVNRV VLDITSKPPA TIEWE

References

[1]

"Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM408590 Genomic DNA. Translation: CAL73455.1.
RefSeq	YP_979545.1. NC_008769.1.
3D structure databases
ProteinModelPortal	A1KP87.
SMR	A1KP87. Positions 17-525.
ModBase	Search...
Protein-protein interaction databases
STRING	410289.BCG_3466c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL73455; CAL73455; BCG_3466c.
GeneID	4698540.
KEGG	mbb:BCG_3466c.
PATRIC	18018068. VBIMycBov80988_3776.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0519.
HOGENOM	HOG000223964.
KO	K01951.
OMA	SLVWMSH.
ProtClustDB	PRK00074.
Enzyme and pathway databases
BioCyc	MBOV410289:GJW7-3509-MONOMER.
UniPathway	UPA00189; UER00296.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_00344. GMP_synthase.
InterPro	IPR017926. GATASE_1. IPR001674. GMP_synth_C. IPR004739. GMP_synth_N. IPR022955. GMP_synthase. IPR025777. GMPS_ATP_PPase_dom. IPR022310. NAD/GMP_synthase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00117. GATase. 1 hit. PF00958. GMP_synt_C. 1 hit. PF02540. NAD_synthase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00884. guaA_Cterm. 1 hit. TIGR00888. guaA_Nterm. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. PS51553. GMPS_ATP_PPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUAA_MYCBP

Accession

Primary (citable) accession number: A1KP87

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program