Reviewed, UniProtKB/Swiss-Prot Q63RL3 (URE1_BURPS)

Names and origin

Protein names

Recommended name:
    Urease subunit alpha
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit alpha

Gene names

Name:	ureC
Ordered Locus Names:	BPSL2659

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Urea + H2O = CO2 + 2 NH3. HAMAP MF_01953
Cofactor	Binds 2 nickel ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP MF_01953
Subunit structure	Heterotrimer of ureA (gamma), ureB (beta) and ureC (alpha) subunits. Three heterotrimers associate to form the active enzyme By similarity.
Subcellular location	Cytoplasm By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two nickel ions By similarity.
Sequence similarities	Belongs to the urease family. Contains 1 urease domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Nickel
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	urea metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW urease 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 – 568	568	Urease subunit alpha HAMAP MF_01953		PRO_0000234148
Regions
	Domain	130 – 568	439	Urease
Sites
	Active site	321	1	Proton donor By similarity
	Metal binding	135	1	Nickel 2 By similarity
	Metal binding	137	1	Nickel 2 By similarity
	Metal binding	218	1	Nickel 1; via carbamate group By similarity
	Metal binding	218	1	Nickel 2; via carbamate group By similarity
	Metal binding	247	1	Nickel 1 By similarity
	Metal binding	273	1	Nickel 1 By similarity
	Metal binding	361	1	Nickel 2 By similarity
	Binding site	220	1	Substrate By similarity
Amino acid modifications
	Modified residue	218	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63RL3-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 351B1622B0E806DE	FASTA	568	60,736
	10 20 30 40 50 60 MTLRLSRRAY AEMYGPTTGD RIRLADTELL IEVERDHTLY GEEVKFGGGK VIRDGMGQSQ 70 80 90 100 110 120 LPAADVADTV ITNAVILDHW GIVKADIAIK HGRIAAIGKA GNPDIQPGVT IAIGAATEII 130 140 150 160 170 180 AGEGLIVTAG GIDTHIHFIS PQQIDEALAS GVTTMIGGGT GPATGTNATT CTPGPWHMER 190 200 210 220 230 240 MLQAADGWPI NLGFLGKGNA SRPQPLVEQI EAGAIGLKLH EDWGTTPAAI DNCLTVADDT 250 260 270 280 290 300 DTQVAIHTDT LNEAGFVEAT VAAFKGRTIH TYHTEGAGGG HAPDILKVCG EANVLPSSTN 310 320 330 340 350 360 PTRPYTINTL DEHLDMLMVC HHLDPSIAED LAFAESRIRR ETIAAEDILH DLGALSMLSS 370 380 390 400 410 420 DSQAMGRVGE VIIRTWQTAH KMKVQRGALT GDGARNDNFR AKRYVAKYTI NPALTHGIAH 430 440 450 460 470 480 EVGSIEPGKW ADLVLWEPAF FGVKPAMIIK GGMIAVAQMG DPNASIPTPQ PVHYREMFAT 490 500 510 520 530 540 RGGALARTSL TFVSQLALDA GISARYGLAK RLVPVRGCRT VTKRDMIHNA WQPAIRVDPE 550 560 TYDVVADGAL LTCEPAAVLP MAQRYFLF

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571965 Genomic DNA. Translation: CAH36667.1.
RefSeq	YP_109255.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3092913.
GenomeReviews	Gene locus BPSL2659 in contig BX571965_GR.
KEGG	bps:BPSL2659.
NMPDR	fig|272560.3.peg.4918.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63RL3.
OMA	SHIHFIC.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL2659-MON.
BRENDA	3.5.1.5. 275934.
Family and domain databases
HAMAP	MF_01953. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR011612. Urease_alpha_N. IPR005848. Urease_asu. IPR017951. Urease_asu_c. IPR017952. Urease_asu_core. IPR017950. Urease_asu_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. PF00449. Urease_alpha. 1 hit. [Graphical view]
PRINTS	PR01752. UREASE.
TIGRFAMs	TIGR01792. urease_alph. 1 hit.
PROSITE	PS01120. UREASE_1. 1 hit. PS00145. UREASE_2. 1 hit. PS51368. UREASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

URE1_BURPS

Accession

Primary (citable) accession number: Q63RL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 41 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)