O59072 (GUAAB_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GMP synthase [glutamine-hydrolyzing] subunit B
EC=6.3.5.2

Alternative name(s):
GMP synthetase

Gene names

Name:	guaAB
Ordered Locus Names:	PH1347

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	308 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_00345
Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP MF_00345
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP MF_00345
Subunit structure	Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B) Potential.
Sequence similarities	Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
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: 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 – 308

308

GMP synthase [glutamine-hydrolyzing] subunit B HAMAP MF_00345

PRO_0000140249

Regions

Domain

1 – 185

185

GMPS ATP-PPase

Nucleotide binding

28 – 34

7

ATP By similarity

Secondary structure

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308

Helix Strand Turn

Details...

Helix

3 – 18

16

Beta strand

23 – 26

4

Helix

31 – 44

14

Helix

45 – 47

3

Beta strand

48 – 54

7

Helix

62 – 70

9

Turn

71 – 74

4

Beta strand

77 – 82

6

Helix

84 – 90

7

Turn

91 – 93

3

Helix

97 – 119

23

Beta strand

122 – 125

4

Beta strand

156 – 158

3

Turn

160 – 163

4

Helix

166 – 175

10

Helix

180 – 183

4

Helix

192 – 196

5

Beta strand

197 – 200

4

Helix

203 – 222

20

Beta strand

228 – 234

7

Beta strand

239 – 259

21

Beta strand

261 – 268

8

Helix

273 – 286

14

Beta strand

290 – 296

7

Sequences

	Sequence		Length	Mass (Da)
	O59072 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 8B209770605AE4BA	FASTA	308	34,562
	10 20 30 40 50 60 MDWGRFVEEK VREIRETVGD SKAIIALSGG VDSSTAAVLA HKAIGDRLHA VFVNTGFLRK 70 80 90 100 110 120 GEPEFVVKTF RDEFGMNLHY VDAQDRFFSA LKGVTDPEEK RKIIGRVFIE VFEEVAKKIG 130 140 150 160 170 180 AEYLIQGTIA PDWIESQGKI KSHHNVGGLP EKLNLKLIEP LRDLYKDEVR ELAKFLGLPE 190 200 210 220 230 240 KIYNRMPFPG PGLAVRVIGE VTPEKIRIVR EANAIVEEEV ERAGLRPWQA FAVLLGVKTV 250 260 270 280 290 300 GVQGDIRAYK ETIAVRIVES IDGMTANAMN VPWEVLQRIA FRITSEIPEV GRVLYDITNK PPATIEFE

References

	« Hide 'large scale' referencesShow 'large scale' 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: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]	"Crystal structure of the GMP synthase from Pyrococcus horikoshii OT3." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30453.1.

PIR

E71006.

RefSeq

NP_143230.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DPL	X-ray	1.43	A/B	1-308	[»]
3A4I	X-ray	1.79	A/B	1-308	[»]

ProteinModelPortal

O59072.

SMR

O59072. Positions 1-308.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000001115; EBPYRP00000001115; EBPYRG00000001115.

GeneID

1443673.

GenomeReviews

Gene locus PH1347 in contig BA000001_GR.

KEGG

pho:PH1347.

NMPDR

fig|70601.1.peg.1326.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022268.

HOGENOM

HBG391775.

OMA

QGTIAPD.

PhylomeDB

O59072.

ProtClustDB

PRK00919.

Enzyme and pathway databases

BioCyc

PHOR70601:PH1347-MONOMER.

Family and domain databases

HAMAP

MF_00345. GMP_synthase_B.
[Tree]

InterPro

IPR001674. GMP_synth_C.
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

PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 2 hits.
[Graphical view]

TIGRFAMs

TIGR00884. GuaA_Cterm. 1 hit.

PROSITE

PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUAAB_PYRHO

Accession

Primary (citable) accession number: O59072

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program