Q9L0H2 (GUAA_STRCO) 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:	SCO4785
ORF Names:	SCD63.17

Organism

Streptomyces coelicolor

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	526 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 Reference 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 – 526	526	GMP synthase [glutamine-hydrolyzing] HAMAP MF_00344		PRO_0000140186
Regions
	Domain	13 – 204	192	Glutamine amidotransferase type-1
	Domain	205 – 400	196	GMPS ATP-PPase
	Nucleotide binding	232 – 238	7	ATP By similarity
Sites
	Active site	90	1	Nucleophile By similarity
	Active site	178	1	By similarity
	Active site	180	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9L0H2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 43ACC404EE19EEA3	FASTA	526	56,613
	10 20 30 40 50 60 MSSATPAAAA PDTVLVVDFG AQYAQLIARR VREARVYSEI VPSSMPVEEI LAKNPAAIIL 70 80 90 100 110 120 SGGPSSVYEA GAPTLDRSLF EAGVPVFGMC YGFQLMAQTL GGTVDNSGAR EYGRTELAVS 130 140 150 160 170 180 KPSSTLFEGT PAEQSVWMSH GDACSAAPEG FTVTGSTDVV PVAAFENDEK KLYGVQYHPE 190 200 210 220 230 240 VMHSTHGQQV LEHFLYRGAG LSPDWTTGNV IEEQVAAIRA QVGDRRAICG LSGGVDSAVA 250 260 270 280 290 300 AALVQKAIGS QLTCVYVDHG LMRKGETEQV EKDFVAATGV QLKVVDASER FLGALAGVSD 310 320 330 340 350 360 PEQKRKIIGR EFIRVFEQAQ LEIMREDGPE VAFLVQGTLY PDVVESGGGT GTANIKSHHN 370 380 390 400 410 420 VGGLPDDIEF ELVEPLRQLF KDEVRMVGQE LGLPDEIVQR QPFPGPGLGI RIVGEVTKER 430 440 450 460 470 480 LDLLREADAI AREELTAAGL DRDIWQCPVV LLADVRSVGV QGDGRTYGHP IVLRPVSSED 490 500 510 520 AMTADWSRLP YEVLSKISTR ITNEVTDVNR VVLDVTSKPP GTIEWE

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939121 Genomic DNA. Translation: CAB82024.1.
RefSeq	NP_628943.1. NC_003888.3.
3D structure databases
ProteinModelPortal	Q9L0H2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1100226.
GenomeReviews	Gene locus SCO4785 in contig AL645882_GR.
KEGG	sco:SCO4785.
NMPDR	fig|100226.1.peg.4740.
PATRIC	23739398. VBIStrCoe124346_4859.
Phylogenomic databases
HOGENOM	HBG391775.
OMA	DGRTYEY.
PhylomeDB	Q9L0H2.
ProtClustDB	PRK00074.
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_STRCO

Accession

Primary (citable) accession number: Q9L0H2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program