Reviewed, UniProtKB/Swiss-Prot Q5P9L5 (GUAA_ANAMM)

Names and origin

Protein names

Recommended name:
    GMP synthase [glutamine-hydrolyzing]
    EC=6.3.5.2
Alternative name(s):
    Glutamine amidotransferase
    GMP synthetase

Gene names

Name:	guaA
Ordered Locus Names:	AM1188

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 MF_00344
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP MF_00344
Subunit structure	Homodimer By similarity.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain. Contains 1 GMP-binding 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: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP GMP synthase (glutamine-hydrolyzing) 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 – 529	529	GMP synthase [glutamine-hydrolyzing] HAMAP MF_00344		PRO_0000229398
Regions
	Domain	3 – 205	203	Glutamine amidotransferase type-1
	Domain	236 – 396	161	GMP-binding
	Nucleotide binding	232 – 238	7	ATP By similarity
Sites
	Active site	87	1	Nucleophile By similarity
	Active site	179	1	By similarity
	Active site	181	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P9L5-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: FDECF79E00FE3195	FASTA	529	57,685
	10 20 30 40 50 60 MSTVAIVDFG SQVTQLIARR VRELGVYSEV FPPSTDFQAM ASRGIKIDAF ILSGGPNSVQ 70 80 90 100 110 120 QLHGVPNAVS DVLNLNLQKG VPVLGICYGF QMLAHYFGAD VAQSVAREFG RAWLDVIEPS 130 140 150 160 170 180 SITEGVWSLG SKVDVWMSHS DSIVGEVPQG FRVVARSADT GAVAFMCNDE RKIYGVQFHP 190 200 210 220 230 240 EVAHTPGGRE MLDNFLKIAG CTRDWTMGSF LHTQIGAIKS ATDGGRVVAA ISGGVDSSVA 250 260 270 280 290 300 SVLVHKAIGE RLVCVFVDTG LLRKGEAGVV RDLFVGKLNM HVNVLDKSAL FMQRLAGVQD 310 320 330 340 350 360 PEVKRKIIGE TFIEVFEQEA KSLGDIKFLM QGTIYPDVIE SGVGESGTKI KSHHNVGGLP 370 380 390 400 410 420 EIMNLSLVEP LRHLFKDEVR LLGKELGLPS AILDRHPFPG PGLAVRIMGE VTAERVELLR 430 440 450 460 470 480 EIDNIYIDMM RDSGLYDHIW QAFAVLVPVR TVGVMGDGRT YGYVCALRAV TSSDGMTADC 490 500 510 520 FPFGETDERK LEFLAFLQKV SRAIVSNLQG VNRVVYDMTS KPPATIEWE

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000030 Genomic DNA. Translation: AAV87015.1.
RefSeq	YP_154270.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P9L5.
Genome annotation databases
GeneID	3171301.
GenomeReviews	Gene locus AM1188 in contig CP000030_GR.
KEGG	ama:AM1188.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5P9L5.
OMA	NEGDMVM.
Enzyme and pathway databases
BioCyc	AMAR234826:AM1188-MON.
Family and domain databases
HAMAP	MF_00344. [Tree]
InterPro	IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. IPR001674. GMP_synth_C. IPR004739. GMP_synth_N. IPR014729. Rossmann-like_a/b/a_fold. IPR018318. tRNA_MeTrfase-like. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
Pfam	PF00117. GATase. 1 hit. PF00958. GMP_synt_C. 1 hit. PF03054. tRNA_Me_trans. 1 hit. [Graphical view]
PRINTS	PR00096. GATASE.
TIGRFAMs	TIGR00884. guaA_Cterm. 1 hit. TIGR00888. guaA_Nterm. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUAA_ANAMM

Accession

Primary (citable) accession number: Q5P9L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	January 4, 2005
Last modified:	November 3, 2009
This is version 35 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)