A3MMV2 (URE1_BURM7) Reviewed, UniProtKB/Swiss-Prot

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:	BMA10247_2057

Organism

Burkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]

Taxonomic identifier

320389 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
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. HAMAP MF_01953
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 HAMAP MF_01953.
Post-translational modification	Carbamylation allows a single lysine to coordinate two nickel ions By similarity. HAMAP MF_01953
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nickel cation binding Inferred from electronic annotation. Source: InterPro urease 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 – 568	568	Urease subunit alpha HAMAP MF_01953		PRO_1000070649
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)
	A3MMV2 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: C50CC452A29563CC	FASTA	568	60,662
	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 KMKVQRGALA GDGARNDNFR AKRYVAKYTI NPALTHGIAH 430 440 450 460 470 480 EVGSIEPGKW ADLVLWEPAF FGVKPAMIVK GGMIAVAQMG DPNASIPTPQ PVHYREMFAT 490 500 510 520 530 540 RGGALARTSL TFVSQLALDA GIGARYGLAK RLVPVRGCRT VTKRDMIHNA WQPAIRVDPE 550 560 TYDVVADGAL LTCEPAAVLP MAQRYFLF

References

[1]	DeShazer D., Woods D.E., Nierman W.C. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 10247.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000548 Genomic DNA. Translation: ABO04242.1.
RefSeq	YP_001081588.1. NC_009080.1.
3D structure databases
ProteinModelPortal	A3MMV2.
SMR	A3MMV2. Positions 5-568.
ModBase	Search...
Protein-protein interaction databases
STRING	A3MMV2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4891555.
GenomeReviews	Gene locus BMA10247_2057 in contig CP000548_GR.
KEGG	bmn:BMA10247_2057.
PATRIC	19146501. VBIBurMal96640_4286.
TIGR	BMA10247_2057.
Phylogenomic databases
HOGENOM	HBG357507.
OMA	TIHAFHT.
ProtClustDB	PRK13207.
Enzyme and pathway databases
BioCyc	BMAL320389:BMA10247_2057-MONOMER.
Family and domain databases
HAMAP	MF_01953. Urease_alpha. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR011059. Metal-dep_hydrolase_composite. IPR011612. Urease_alpha_N. IPR005848. Urease_asu. IPR017951. Urease_asu_c. IPR017950. Urease_asu_CS. [Graphical view]
KO	K01428.
Pfam	PF01979. Amidohydro_1. 1 hit. PF00449. Urease_alpha. 1 hit. [Graphical view]
PRINTS	PR01752. UREASE.
SUPFAM	SSF51338. Metalo_hydrolase. 2 hits.
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_BURM7

Accession

Primary (citable) accession number: A3MMV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	April 3, 2007
Last modified:	December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program