P44335 (GUAA_HAEIN) 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:	HI_0222

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	523 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 – 523	523	GMP synthase [glutamine-hydrolyzing] HAMAP MF_00344		PRO_0000140131
Regions
	Domain	8 – 205	198	Glutamine amidotransferase type-1
	Domain	206 – 398	193	GMPS ATP-PPase
	Nucleotide binding	233 – 239	7	ATP By similarity
Sites
	Active site	85	1	Nucleophile By similarity
	Active site	179	1	By similarity
	Active site	181	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44335 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 6361F38BC20CF154	FASTA	523	58,186
	10 20 30 40 50 60 MTNIHYHKIL ILDFGSQYTQ LIARRVREIG VYCELWAWDV TEQQIREFAP TGIILSGSPE 70 80 90 100 110 120 STTEENSPRA PEYVFNAGVP VLGICYGMQT MAMQLGGLTE TSDHREFGYA SVSLENSTAL 130 140 150 160 170 180 FANLNDNLTA SEPKLDVWMS HGDKVTRLPE NFKVTGTTLT CPIAAMSDES RRFYGVQFHP 190 200 210 220 230 240 EVTHTKKGLE LLTNFVVNIC GCETKWTAEN IIEDAVARIK EQVGDDEVIL GLSGGVDSSV 250 260 270 280 290 300 VALLLHRAIG KNLHCVFVDN GLLRLHEGDQ VMEMFGDKFG LNITRVDAES RFLGELAGVS 310 320 330 340 350 360 DPEAKRKIIG KVFVDVFDDE SKKLTNVKWL AQGTIYPDVI ESAASKTGKA HVIKSHHNVG 370 380 390 400 410 420 GLPDYMKLGL VEPLRELFKD EVRKIGLALG LPAEMINRHP FPGPGLGVRV LGEVKKEYCD 430 440 450 460 470 480 LLRRADAIFI EELRNSGWYE KTSQAFSVFL PVKSVGVMGD GRKYDWVISL RAVETIDFMT 490 500 510 520 AHWAHLPYDL LGKVSNRIIN EVNGISRVVY DISGKPPATI EWE

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC21891.1.
PIR	I64055.
RefSeq	NP_438394.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44335.
SMR	P44335. Positions 3-523.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	951140.
GenomeReviews	Gene locus HI_0222 in contig L42023_GR.
KEGG	hin:HI0222.
NMPDR	fig|71421.1.peg.212.
PATRIC	20188965. VBIHaeInf48452_0235.
TIGR	HI_0222.
Phylogenomic databases
HOGENOM	HBG391775.
OMA	DGRTYEY.
PhylomeDB	P44335.
ProtClustDB	PRK00074.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0222-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_HAEIN

Accession

Primary (citable) accession number: P44335

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program