Q7VRS6 (URE1_BLOFL) 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:	Bfl523

Organism

Blochmannia floridanus [Complete proteome] [HAMAP]

Taxonomic identifier

203907 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

Protein attributes

Sequence length	567 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 – 567	567	Urease subunit alpha HAMAP MF_01953		PRO_0000234134
Regions
	Domain	129 – 567	439	Urease
Sites
	Active site	320	1	Proton donor By similarity
	Metal binding	134	1	Nickel 2 By similarity
	Metal binding	136	1	Nickel 2 By similarity
	Metal binding	217	1	Nickel 1; via carbamate group By similarity
	Metal binding	217	1	Nickel 2; via carbamate group By similarity
	Metal binding	246	1	Nickel 1 By similarity
	Metal binding	272	1	Nickel 1 By similarity
	Metal binding	360	1	Nickel 2 By similarity
	Binding site	219	1	Substrate By similarity
Amino acid modifications
	Modified residue	217	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VRS6 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: D100D0F7DD327E09	FASTA	567	61,658
	10 20 30 40 50 60 MNMLNKKIYA EMYGPTVGDS VRLADTDLWV KIEKDFTIYG EEVKFGGGKV IRDGMGQGQM 70 80 90 100 110 120 NNKECVDLVL TNAIIIDYWG VIKADIGINN GRIVGIGKSG NPDIQPGVTI YIGPGTEVIS 130 140 150 160 170 180 AEGKIVTAGG IDVHVHFICP QQIEEALSSG MTTLIGGGTG PTTGSNATTC TPGVWFISRM 190 200 210 220 230 240 LQAADALPIN IGFTGKGSSA LPESLIEQIH AGAIGLKVHE DWGATPATID CCLNVADNFD 250 260 270 280 290 300 VQVSIHTDTL NESGFLETTI SAIKNRTIHA YHVEGAGGGH SPDIIRICEL NNVLPSSTNP 310 320 330 340 350 360 TLPYTINTVD EHLDMMMVCH NLNCNLPEDI AFAESRIRRE TIAAEDILHD LGALSMISSD 370 380 390 400 410 420 SQAMGRIGET ILRTWQTAHK MKLQRGSLLG DDQYNDNTRI KRYIAKYTIN PAITHGIAHE 430 440 450 460 470 480 VGSVEIGKLA DLVLWSPVFF GVKPELIVKG GMIVSSVMGD PNASIPTPQP VYYRLMFGSY 490 500 510 520 530 540 DLAKCATRMT FISQSSYDVG VVENLRLNSL IGISKRCRNI KKDHMINNNL KPVMEVDPQT 550 560 YEVRANGELL VCEPVSVVPM SQRYFLF

References

[1]

"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes." Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed: 12886019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248583 Genomic DNA. Translation: CAD83209.1.
RefSeq	NP_878803.1. NC_005061.1.
3D structure databases
ProteinModelPortal	Q7VRS6.
SMR	Q7VRS6. Positions 4-567.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7VRS6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1499723.
GenomeReviews	Gene locus Bfl523 in contig BX248583_GR.
KEGG	bfl:Bfl523.
PATRIC	31964659. VBICanBlo38691_0509.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0804.
HOGENOM	HBG357507.
OMA	TIHAFHT.
ProtClustDB	PRK13207.
Enzyme and pathway databases
BioCyc	CBLO203907:BFL523-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_BLOFL

Accession

Primary (citable) accession number: Q7VRS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program