Reviewed, UniProtKB/Swiss-Prot Q7VUD3 (URE1_BORPE)

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:	BP3168

Organism

Bordetella pertussis [Complete proteome] [HAMAP]

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	571 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 – 571	571	Urease subunit alpha HAMAP MF_01953		PRO_0000234137
Regions
	Domain	134 – 571	438	Urease
Sites
	Active site	325	1	Proton donor By similarity
	Metal binding	139	1	Nickel 2 By similarity
	Metal binding	141	1	Nickel 2 By similarity
	Metal binding	222	1	Nickel 1; via carbamate group By similarity
	Metal binding	222	1	Nickel 2; via carbamate group By similarity
	Metal binding	251	1	Nickel 1 By similarity
	Metal binding	277	1	Nickel 1 By similarity
	Metal binding	365	1	Nickel 2 By similarity
	Binding site	224	1	Substrate By similarity
Amino acid modifications
	Modified residue	222	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VUD3-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 26C0C1BEA5870D66	FASTA	571	60,617
	10 20 30 40 50 60 MTRISRSAYA EIYGPTVVGG VGDRVRLADT LLLAEVEKDH TIFGEEVKFG GGKVIRDGMG 70 80 90 100 110 120 QSQRLATDCV DTVITNALII DAVTGIVKAD IGIKDGLISG IGKAGNPDTQ PGVTIIIGAS 130 140 150 160 170 180 TEVVAGEGLI VTAGAIDTHI HFICPQQIEE ALATGTTTMI GGGTGPATGS LATTSTSGPW 190 200 210 220 230 240 HMAAMLQALD AFPVNVGLFG KGSSSSHGAL LEQVRAGAMG LKIHEDWAST PASIDTCLNV 250 260 270 280 290 300 AEETDIQVAI HSDTLNESGF VEDTFAAFKG RTIHSFHTEG AGGGHAPDII RAAGMPNVLP 310 320 330 340 350 360 ASTNPTMPFT RNTIDEHLDM VMVCHHLDPS IAEDLAFAES RIRRETIAAE DILHDLGAFS 370 380 390 400 410 420 IMSSDSQAMG RVGEIVLRTW QTAHKMKLQR GPLQGDSERS DNERIKRYIA KYTINPAVAH 430 440 450 460 470 480 GIAHLVGSVE VGKLADLVLW KPAFFGVKVN MVLKSGMAVS ASIGDMGASI STPQPVQIRP 490 500 510 520 530 540 MWGSHGKALR TSVAFVSQVS LSNPAVSELG LNKRLEAVRG CRGVTKHDMV RNNWLPAISV 550 560 570 DPQTYQVYAD GQLLRCEALA ELPMAQRYFL F

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640420 Genomic DNA. Translation: CAE43436.1.
RefSeq	NP_881730.1.
3D structure databases
HSSP	HSSP built from PDB template 1EJX based on UniProtKB P18314.
ModBase	Search...
Protein family/group databases
MEROPS	M38.982.
Genome annotation databases
GeneID	2667492.
GenomeReviews	Gene locus BP3168 in contig BX470248_GR.
KEGG	bpe:BP3168.
NMPDR	fig|257313.1.peg.2801.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7VUD3.
OMA	SHIHFIC.
Enzyme and pathway databases
BioCyc	BPER257313:BP3168-MON.
BRENDA	3.5.1.5. 21511.
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_BORPE

Accession

Primary (citable) accession number: Q7VUD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 43 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)