Q82HM9 (GUAA_STRAW) 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:	SAV_3479

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

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. HAMAP MF_00344
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. HAMAP MF_00344
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: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GMP synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC
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 MF_00344		PRO_0000140185
Regions
	Domain	12 – 203	192	Glutamine amidotransferase type-1
	Domain	204 – 399	196	GMPS ATP-PPase
	Nucleotide binding	231 – 237	7	ATP By similarity
Sites
	Active site	89	1	Nucleophile By similarity
	Active site	177	1	By similarity
	Active site	179	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82HM9 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 8513779A66581A93	FASTA	525	56,785
	10 20 30 40 50 60 MPSAPSAAAP DTVLVVDFGA QYAQLIARRV REARVYSEIV PSTMPVAEML AKNPAAIILS 70 80 90 100 110 120 GGPSSVYAEG APRLDREIFE AGVPVFGMCY GFQLMATTLG GTVDNTGARE YGRTPLHVSK 130 140 150 160 170 180 SGSTLFEGTP DEQPVWMSHG DACSAAPEGF TVTASTDVVP VAAFENDEKR LYGVQYHPEV 190 200 210 220 230 240 MHSTHGQQVL EHFLYRGAGL TPSWTTGNVI DEQVELIREQ VGTRRAICGL SGGVDSAVAA 250 260 270 280 290 300 ALVQKAIGSQ LTCVYVDHGL MRQGETEQVE KDFVAATGVQ LKVVDAEERF LTALKGVSDP 310 320 330 340 350 360 EEKRKIIGRE FIRVFEQAQA EIIADEGPEV AFLVQGTLYP DVVESGGGTG TANIKSHHNV 370 380 390 400 410 420 GGLPEDLEFE LIEPLRKLFK DEVRMVGQEL GLPDEIVQRQ PFPGPGLGIR IVGEVTKERL 430 440 450 460 470 480 DLLREADAIA REELTAAGLD REIWQCPVVL LADVRSVGVQ GDGRTYGHPI VLRPVSSEDA 490 500 510 520 MTADWSRLPY DTLAKISTRI TNEVADVNRV VLDVTSKPPG TIEWE

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC71191.1.
RefSeq	NP_824656.1. NC_003155.4.
3D structure databases
ProteinModelPortal	Q82HM9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1210748.
GenomeReviews	Gene locus SAV_3479 in contig BA000030_GR.
KEGG	sma:SAV_3479.
NMPDR	fig|227882.1.peg.3482.
PATRIC	23720625. VBIStrAve112782_3719.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG391775.
OMA	DGRTYEY.
ProtClustDB	PRK00074.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV3479-MONOMER.
Family and domain databases
HAMAP	MF_00344. GMP_synthase. [Tree]
InterPro	IPR017926. GATASE_1. IPR001674. GMP_synth_C. IPR004739. GMP_synth_N. IPR022955. GMP_synthase. IPR022310. NAD/GMP_synthase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01951.
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_STRAW

Accession

Primary (citable) accession number: Q82HM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program