A3N2R4 (URE1_ACTP2) 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:	APL_1616

Organism

Actinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]

Taxonomic identifier

416269 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	572 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 – 572	572	Urease subunit alpha HAMAP MF_01953		PRO_1000070642
Regions
	Domain	136 – 572	437	Urease
Sites
	Active site	327	1	Proton donor By similarity
	Metal binding	141	1	Nickel 2 By similarity
	Metal binding	143	1	Nickel 2 By similarity
	Metal binding	224	1	Nickel 1; via carbamate group By similarity
	Metal binding	224	1	Nickel 2; via carbamate group By similarity
	Metal binding	253	1	Nickel 1 By similarity
	Metal binding	279	1	Nickel 1 By similarity
	Metal binding	367	1	Nickel 2 By similarity
	Binding site	226	1	Substrate By similarity
Amino acid modifications
	Modified residue	224	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3N2R4 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 112EC338450B5F55	FASTA	572	61,835
	10 20 30 40 50 60 MALTIPRSQY VATYGPTVGD KVRLGDTDLW ATIEQDFLTK GDECKFGGGK SVRDGMAQSS 70 80 90 100 110 120 TSTRDNPNVL DFALTNVMII DAKLGIIKAD IGIRDGRIVG IGQAGNPDTM DNVTPNMIIG 130 140 150 160 170 180 ASTEVHNGAH LIATAGGIDT HIHWICPQQA QHAIENGITT MIGGGSGPAD GTHATTCTPG 190 200 210 220 230 240 KFNIERMFQA CEALPVNIGF FGKGNCSMLE PLKEQVVAGA LGLKIHEDWG ATPAVIDAAL 250 260 270 280 290 300 KVADEMDVQV AIHTDTLNES GFLEDTMKAI NGRVIHTFHT EGAGGGHAPD IIKAAMYPNV 310 320 330 340 350 360 LPASTNPTRP FTVNTIDEHL DMLMVCHHLD KRVPEDVAFA DSRIRPETIA AEDILHDMGV 370 380 390 400 410 420 FSIMSSDSQA MGRVGEVVTR TWQTADKMKA QRGALGDEGN DNFRIKRYIA KYTINPAIAH 430 440 450 460 470 480 GISQYVGSLE VGKLADIVLW KPQFFGVKPE FVMKKGFISF AKMGDPNASI PTPQPVFYRP 490 500 510 520 530 540 MFGANAKANT ESAVYFVSQA SVDANIKAQY GIQKETLAVK GCRDVGKKDL VHNNATPEIT 550 560 570 VDPERYEVRV DGEHITCEPA TKVPLAQRYF LF

References

[1]	"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)." Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E. J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L20.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000569 Genomic DNA. Translation: ABN74700.1.
RefSeq	YP_001054305.1. NC_009053.1.
3D structure databases
ProteinModelPortal	A3N2R4.
SMR	A3N2R4. Positions 5-572.
ModBase	Search...
Protein-protein interaction databases
STRING	A3N2R4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4850391.
GenomeReviews	Gene locus APL_1616 in contig CP000569_GR.
KEGG	apl:APL_1616.
PATRIC	20748265. VBIActPle94089_1682.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0804.
HOGENOM	HBG357507.
OMA	MPYTINT.
ProtClustDB	PRK13207.
Enzyme and pathway databases
BioCyc	APLE416269:APL_1616-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_ACTP2

Accession

Primary (citable) accession number: A3N2R4

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