Reviewed, UniProtKB/Swiss-Prot Q8YHZ8 (URE12_BRUME)

Names and origin

Protein names

Recommended name:
    Urease subunit alpha 2
    EC=3.5.1.5
Alternative name(s):
    Urea amidohydrolase subunit alpha 2

Gene names

Name:	ureC2
Ordered Locus Names:	BMEI0647

Organism

Brucella melitensis [Complete proteome] [HAMAP]

Taxonomic identifier

29459 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	573 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. HAMAP MF_01953
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: 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 – 573	573	Urease subunit alpha 2 HAMAP MF_01953		PRO_0000234144
Regions
	Domain	135 – 573	439	Urease
Sites
	Active site	326	1	Proton donor By similarity
	Metal binding	140	1	Nickel 2 By similarity
	Metal binding	142	1	Nickel 2 By similarity
	Metal binding	223	1	Nickel 1; via carbamate group By similarity
	Metal binding	223	1	Nickel 2; via carbamate group By similarity
	Metal binding	252	1	Nickel 1 By similarity
	Metal binding	278	1	Nickel 1 By similarity
	Metal binding	366	1	Nickel 2 By similarity
	Binding site	225	1	Substrate By similarity
Amino acid modifications
	Modified residue	223	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YHZ8-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: A297E706F15A490B	FASTA	573	60,785
	10 20 30 40 50 60 MTQISRQQYA DLYGPTIGDK IRLGDSDLYV EIEKDLRATY GDELQYGGGK TLRDGMGSEN 70 80 90 100 110 120 FLTQEAGCLD LVITNVTVID AIQGVVKADV GIRNGRIVGL GKAGNPSTMD GVTRGLVTGA 130 140 150 160 170 180 STDAISGEHL ILTAGGMDTH VHYIAPQQVE AALSNGITTL WGGGIGPVDG TNGVTTTNGP 190 200 210 220 230 240 WNLEMMLRSI EGLPINFGIQ GKGNSTGIAP LIEQLEAGAA GFKVHEDYGA TPATIRACLS 250 260 270 280 290 300 VADEYDVSVA VHTDTLNESG YVEDTIAAFD GRSVHTYHSE GAGGGHAPDL LKVVGQNNIL 310 320 330 340 350 360 PSSTNPTLPC GKNSVAELFD MIMVCHNLNP RIPSDVAFAE SRVRAETIVA ESVLHDMGAI 370 380 390 400 410 420 SMIGSDSQAM GRIGETYLRA IQTADAMKKA RGPLPEDAPG NDNFRVLRYI AKVTINPALT 430 440 450 460 470 480 AGVGDVIGSI ESGKFADLVL WEPAFFGVKP KLVLKGGLVA WANMGDPNAS LPTPQPMYYR 490 500 510 520 530 540 PMFAAYGSAL QKTSITFVSR AAYDKGVADR FGLQRLVMPV SGTRVIGKAH MVRNSYLPNI 550 560 570 EVDPQTFAVK VDGVHATVKP PQSISLNQLY FFS

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: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008917 Genomic DNA. Translation: AAL51828.1.
PIR	AI3332.
RefSeq	NP_539564.1.
3D structure databases
SMR	Q8YHZ8. Positions 2-572.
ModBase	Search...
Protein family/group databases
MEROPS	M38.982.
Genome annotation databases
GeneID	1196358.
GenomeReviews	Gene locus BMEI0647 in contig AE008917_GR.
KEGG	bme:BMEI0647.
NMPDR	fig|224914.1.peg.646.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG357507.
OMA	YGINSQA.
Enzyme and pathway databases
BioCyc	BMEL224914:BMEI0647-MONOMER.
BRENDA	3.5.1.5. 277959.
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. 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

URE12_BRUME

Accession

Primary (citable) accession number: Q8YHZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	March 1, 2002
Last modified:	February 9, 2010
This is version 60 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)