Q8YF72 (URE11_BRUME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Urease subunit alpha 1
EC=3.5.1.5

Alternative name(s):
Urea amidohydrolase subunit alpha 1

Gene names

Name:	ureC1
Ordered Locus Names:	BMEI1652

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella melitensis › Brucella melitensis bv. 1

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Urea + H2O = CO2 + 2 NH3. HAMAP-Rule 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-Rule 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. HAMAP-Rule 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 catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nickel cation binding Inferred from electronic annotation. Source: HAMAP 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 – 570	570	Urease subunit alpha 1 HAMAP-Rule MF_01953		PRO_0000234143
Regions
	Domain	131 – 570	440	Urease
Sites
	Active site	322	1	Proton donor By similarity
	Metal binding	136	1	Nickel 2 By similarity
	Metal binding	138	1	Nickel 2 By similarity
	Metal binding	219	1	Nickel 1; via carbamate group By similarity
	Metal binding	219	1	Nickel 2; via carbamate group By similarity
	Metal binding	248	1	Nickel 1 By similarity
	Metal binding	274	1	Nickel 1 By similarity
	Metal binding	362	1	Nickel 2 By similarity
	Binding site	221	1	Substrate By similarity
Amino acid modifications
	Modified residue	219	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YF72 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 6487ABAC61D967EC	FASTA	570	61,001
	10 20 30 40 50 60 MPARISRATY AQMFGPTVGD KVRLADTDLI IEVERDLTTY GEEVKFGGGK VIRDGMGQSQ 70 80 90 100 110 120 LSRAEGAMDT VITNALILDH SGIYKADIGL LDGRIALIGK AGNPDTQPGI SIIIGPGTEI 130 140 150 160 170 180 IAGEGKIVTA GGIDTHVHFI SPQQVDEALN AGITCMVGGG TGPAHGTLAT TCTPGPWHIA 190 200 210 220 230 240 RLIQSFDGLP MNIGVFGKGN ASLPGALEEM VRAGACGLKL HEDWGCTPAA IDNCLSVADH 250 260 270 280 290 300 FDVQVAIHTD TLNEGGFVED TLNAFKGRTI HSFHTEGAGG GHAPDIIRVC QYPNVLPAST 310 320 330 340 350 360 NPTRPYTVNT IAEHLDMLMV CHHLSPAIPE DIAFAESRIR KETIAAEDIL HDMGAFSIIS 370 380 390 400 410 420 SDSQAMGRVG EMIIRCWQTA DKMKKQRGSL PDDRPGNDNY RARRYIAKYT INPAIAHGMA 430 440 450 460 470 480 HEIGSVEVGK RADLVLWNSA FFGVKPDMVL LGGWIATAPM GDANGSIPTP QPMHTRPMFG 490 500 510 520 530 540 SFGKALTNTS ITFVSQAAMD EGLREKIGVD KQLVAVVNTR GGIGKHSMIL NNAMPQMEVD 550 560 570 PETYEVRADG ELLTCEPVDV VPMAQRYFLF

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008917 Genomic DNA. Translation: AAL52833.1.
PIR	AF3458.
RefSeq	NP_540569.1. NC_003317.1.
3D structure databases
ProteinModelPortal	Q8YF72.
SMR	Q8YF72. Positions 3-570.
ModBase	Search...
Protein-protein interaction databases
STRING	224914.BMEI1652.
Protein family/group databases
MEROPS	M38.982.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL52833; AAL52833; BMEI1652.
GeneID	1197363.
KEGG	bme:BMEI1652.
PATRIC	17796614. VBIBruMel146950_0128.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000075064.
KO	K01428.
OMA	TIHAFHT.
ProtClustDB	PRK13207.
Enzyme and pathway databases
UniPathway	UPA00258; UER00370.
Family and domain databases
HAMAP	MF_01953. Urease_alpha.
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]
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

URE11_BRUME

Accession

Primary (citable) accession number: Q8YF72

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program