Accession	MF_00344
Dates	1-JUN-2001 (Created) 7-JUN-2008 (Last updated, Version 30)

Data class

Protein

Predictors

HAMAP; MF_00344; [distribution of match scores in UniProtKB];[seed alignment for MF_00344]

Identifier

GUAA

Protein name

RecName: Full=GMP synthase [glutamine-hydrolyzing]; EC=6.3.5.2; AltName: Full=Glutamine amidotransferase; AltName: Full=GMP synthetase;

Gene name

guaA

FUNCTION: Catalyzes the synthesis of GMP from XMP (By similarity).

CATALYTIC ACTIVITY: ATP + xanthosine 5'-phosphate + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate.

PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (glutamine route): step 1/1.

SUBUNIT: Homodimer (By similarity).

SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.

SIMILARITY: Contains 1 GMP-binding domain.

Pfam	PF00117; GATase; 1; PF00958; GMP_synt_C; 1;
PRINTS	PR00096; GATASE; 1;
TIGRFAMs	TIGR00884; guaA_Cterm; 1; TIGR00888; guaA_Nterm; 1;
PROSITE	PS51273; GATASE_TYPE_1; 1; trigger=PRU00605;

Ligase, GMP biosynthesis, Purine biosynthesis, ATP-binding, Nucleotide-binding, Glutamine amidotransferase.

GO:0005524; Molecular function: ATP binding.
GO:0003922; Molecular function: GMP synthase (glutamine-hydrolyzing) activity.
GO:0006177; Biological process: GMP biosynthetic process.

From: GUAA_ECOLI (P04079)
Key		From		To		Description		Condition		FTGroup
DOMAIN		239		401		GMP-binding
NP_BIND		235		241		ATP (By similarity)		S-G-G-[VIT]-D-S-x
ACT_SITE		86		86		Nucleophile (By similarity)		C
ACT_SITE		181		181		By similarity		H
ACT_SITE		183		183		By similarity		E

Size range:	501-551 amino acids
Related UniRules:	MF_00345 (GUAAB); MF_01510 (GUAAA)
Template:	P04079 (GUAA_ECOLI)
Scope:	Bacteria Archaea
Fusion:	Nter: None; Cter: None
Duplicate:	in BACTN
Plasmid encoded:	in BORBU
Comments:	Active site is not conserved in BACHD; CHLPN and the second copy in BACTN have an internal deletion; weird inserts in HELHP, LEPIC and LEPIN; longer N-terminus in RHOBA; all these sequences are not included in alignment and not taken into account in size range. Sequences from AERPE and PYRAE are like that of Eubacteria composed of two domains, while other archaea have separate proteins that correspond to each domain.