Q31F66 (GUAA_THICR) 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:	Tcr_1615

Organism

Thiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]

Taxonomic identifier

317025 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Thiomicrospira › Thiomicrospira crunogena

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.
Catalytic activity	ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP-Rule MF_00344
Pathway	Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP-Rule MF_00344
Subunit structure	Homodimer By similarity.
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: HAMAP glutamine metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP GMP synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP pyrophosphatase activity Inferred from electronic annotation. Source: InterPro
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-Rule MF_00344		PRO_0000229483
Regions
	Domain	10 – 208	199	Glutamine amidotransferase type-1
	Domain	209 – 401	193	GMPS ATP-PPase
	Nucleotide binding	236 – 242	7	ATP By similarity
Sites
	Active site	87	1	Nucleophile By similarity
	Active site	182	1	By similarity
	Active site	184	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q31F66 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 066143A209A2BDE7	FASTA	526	58,693
	10 20 30 40 50 60 MSQNNIHEHR ILILDFGSQY TQLIARRIRE IGVYCEVEPW DIDVEDIVKF GARGIILSGG 70 80 90 100 110 120 PETVTGDNAP VAPVEVFELG VPVLGICYGM QTMAEQLGGK VINATEHEYG YAQVRAHGHT 130 140 150 160 170 180 KLLNDIEDHV TPEGYGMLDV WMSHGDRVDK MPEGFKLMAS TGNCPIAGMA NEEKDFYGIQ 190 200 210 220 230 240 FHPEVTHTTQ GQRMIERFVV DLCGCEKLWT TENIIDDSIA RIRQQVGSDE VLLGLSGGVD 250 260 270 280 290 300 SSVVAALLHK AIGDQLTCVF VDHGLLRHQE GDQVMSMFAE NMGIKVIRVD AEDYFMNALA 310 320 330 340 350 360 GEADPEKKRK IIGHAFIEMF DQESAKLTGV KWLAQGTIYP DVIESAGSKT GKAKVIKSHH 370 380 390 400 410 420 NVGGLPEDMK LELLEPLREL FKDEVRRLGV ALGLPSDMVY RHPFPGPGLG VRILGEVKKE 430 440 450 460 470 480 YADILRLADH IFIEELRAAD LYDKTSQAFT VFLPVKSVGV VGDARRYDYV VSLRAVETID 490 500 510 520 FMTARWAHLP YDFLEKVSNR IINEIPRITR VTYDISSKPP ATIEWE

References

[1]

"The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena XCL-2." Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L., Hauser L.J. , Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E., Zeruth G.T. PLoS Biol. 4:1-17(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: XCL-2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000109 Genomic DNA. Translation: ABB42207.1.
RefSeq	YP_391881.1. NC_007520.2.
3D structure databases
ProteinModelPortal	Q31F66.
SMR	Q31F66. Positions 5-526.
ModBase	Search...
Protein-protein interaction databases
STRING	317025.Tcr_1615.
Proteomic databases
PRIDE	Q31F66.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABB42207; ABB42207; Tcr_1615.
GeneID	3760875.
KEGG	tcx:Tcr_1615.
PATRIC	23975306. VBIThiCru83387_1689.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0519.
HOGENOM	HOG000223964.
KO	K01951.
OMA	YDYVVAL.
ProtClustDB	PRK00074.
Enzyme and pathway databases
UniPathway	UPA00189; UER00296.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_00344. GMP_synthase.
InterPro	IPR017926. GATASE_1. IPR001674. GMP_synth_C. IPR004739. GMP_synth_N. IPR022955. GMP_synthase. IPR025777. GMPS_ATP_PPase_dom. IPR022310. NAD/GMP_synthase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
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_THICR

Accession

Primary (citable) accession number: Q31F66

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program