Reviewed, UniProtKB/Swiss-Prot O59071 (GUAAA_PYRHO)

Names and origin

Protein names

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

Gene names

Name:	guaAA
Ordered Locus Names:	PH1346

Organism

Pyrococcus horikoshii [Complete proteome] [HAMAP]

Taxonomic identifier

53953 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	189 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the synthesis of GMP from XMP By similarity. HAMAP MF_01510
Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP MF_01510
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP MF_01510
Subunit structure	Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B) Potential. HAMAP MF_01510
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure 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: UniProtKB-KW 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 – 189

189

GMP synthase [glutamine-hydrolyzing] subunit A HAMAP MF_01510

PRO_0000140230

Regions

Domain

2 – 189

188

Glutamine amidotransferase type-1

Sites

Active site

79

1

Nucleophile By similarity

Active site

166

1

By similarity

Active site

168

1

By similarity

Secondary structure

1

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189

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

13 – 22

10

Beta strand

26 – 31

6

Helix

36 – 41

6

Beta strand

45 – 49

5

Helix

61 – 66

6

Helix

68 – 70

3

Beta strand

75 – 78

4

Helix

80 – 89

10

Beta strand

92 – 95

4

Beta strand

102 – 109

8

Beta strand

120 – 126

7

Beta strand

129 – 134

6

Beta strand

139 – 147

9

Beta strand

151 – 158

8

Beta strand

160 – 165

6

Helix

175 – 186

12

Sequences

	Sequence		Length	Mass (Da)
	O59071-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 560F55F7A4BB92A7	FASTA	189	21,517
	10 20 30 40 50 60 MMIVIMDNGG QYVHRIWRTL RYLGVETKII PNTTPLEEIK AMNPKGIIFS GGPSLENTGN 70 80 90 100 110 120 CEKVLEHYDE FNVPILGICL GHQLIAKFFG GKVGRGEKAE YSLVEIEIID EDEIFKGLPK 130 140 150 160 170 180 RLKVWESHMD EVKELPPKFK ILARSETCPI EAMKHEELPI YGVQFHPEVA HTEKGEEILR NFAKLCGEL

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OT3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30452.1.

PIR

D71006.

RefSeq

NP_143229.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WL8	X-ray	1.45	A	1-189	[»]
2D7J	X-ray	1.89	A	1-189	[»]

ModBase

Search...

Genome annotation databases

GeneID

1443672.

GenomeReviews

Gene locus PH1346 in contig BA000001_GR.

KEGG

pho:PH1346.

NMPDR

fig|70601.1.peg.1325.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG292341.

OMA

GQYVHRI.

Enzyme and pathway databases

BioCyc

PHOR70601:PH1346-MONOMER.

BRENDA

6.3.5.2. 74679.

Family and domain databases

HAMAP

MF_01510. GMP_synthase_A.
[Tree]

InterPro

IPR006220. Anth_synthII.
IPR001317. CarbamoylP_synth_GATase_dom.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
IPR004739. GMP_synth_N.
[Graphical view]

Pfam

PF00117. GATase. 1 hit.
[Graphical view]

PRINTS

PR00097. ANTSNTHASEII.
PR00099. CPSGATASE.
PR00096. GATASE.

TIGRFAMs

TIGR00888. guaA_Nterm. 1 hit.

PROSITE

PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUAAA_PYRHO

Accession

Primary (citable) accession number: O59071

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	August 1, 1998
Last modified:	February 9, 2010
This is version 64 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)