Reviewed, UniProtKB/Swiss-Prot Q0VKY1 (URE1_ALCBS)

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:	ABO_2719

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	567 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 – 567	567	Urease subunit alpha HAMAP MF_01953		PRO_1000070643
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)
	Q0VKY1-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 4AD6DED981BF1E7F	FASTA	567	60,862
	10 20 30 40 50 60 MATMSRQAYA DMFGPTTGDR VRLADTDLWI QVEKDFTVYG DEVKFGGGKV IRDGMGQSQL 70 80 90 100 110 120 PSAKVMDLVI TNALILDYWG IVKADIGIKN GRIAAIGKAG NPDVQPNVDI IVGPGTDVIA 130 140 150 160 170 180 GEGSIITAGG IDSHIHFICP QQIDEALASG VTTMIGGGTG PTTGTNATTV TPGPWNMARM 190 200 210 220 230 240 LEAADCFPMN LGFLGKGNAS LPESLSEQIS AGAIGLKLHE DWGTTPASID NCLSVAEETD 250 260 270 280 290 300 TQVAIHTDTL NESGFVEDTI AAFKDRTIHT YHTEGAGGGH APDIIRAAGL ANVLPSSTNP 310 320 330 340 350 360 TRPYTVNTAD EHLDMLMVCH HLDPSIPEDV AFAESRIRRE TIAAEDILHD LGAFSMIASD 370 380 390 400 410 420 SQAMGRVGEV VMRTWQTAHK MKVQRGSLKG DPSEHDNFRA KRYVAKYTIN PALAHGMAHE 430 440 450 460 470 480 IGSVEVGKLA DLVLWSPAFF GVKPNLIIKG GMIAMAKMGD PNASIPTPQP VHYRPMFGAY 490 500 510 520 530 540 GKARQATTMT FISQAAMDAG IPEQLTLANR IGVVKGCRTV KKKDMLLNDW LPHLEVDPQT 550 560 YEVRADGQLL TCEPAEVLPM AQRYFLF

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL18167.1.
RefSeq	YP_694439.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VKY1.
Genome annotation databases
GeneID	4211733.
GenomeReviews	Gene locus ABO_2719 in contig AM286690_GR.
KEGG	abo:ABO_2719.
NMPDR	fig|393595.12.peg.2728.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VKY1.
OMA	SHIHFIC.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_2719-MON.
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_ALCBS

Accession

Primary (citable) accession number: Q0VKY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 5, 2006
Last modified:	November 3, 2009
This is version 31 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)