Reviewed, UniProtKB/Swiss-Prot A1TSZ6 (URE1_ACIAC)

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:	Aave_3529

Organism

Acidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]

Taxonomic identifier

397945 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length	572 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 – 572	572	Urease subunit alpha HAMAP MF_01953		PRO_1000070641
Regions
	Domain	134 – 572	439	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)
	A1TSZ6-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 0C3B182FF27064E1	FASTA	572	60,787
	10 20 30 40 50 60 MATVSRRAYA EMFGPTVGDR VRLADTGLVA EVEQDFTLRA GGYGEEVKFG GGKTIRDGMA 70 80 90 100 110 120 QSQRTRAEGA MDTVLTNALV IDHWGIVKAD IGLKDGRVAA IGKAGNPDTQ PGVDIVIGPG 130 140 150 160 170 180 TEIISCEGNI VTAGGIDSHI HFICPQQIEE ALASGITTML GGGTGPATGT LATTCTPGPW 190 200 210 220 230 240 HIERMLQAAD AFPMNIGFLG KGNASLPAAL HEQIEAGVIG LKLHEDWGTT PSAISNCMDV 250 260 270 280 290 300 ADATDTQVAI HSDTLNESGF VENTIAAVGG RGICAFHTEG AGGGHAPDIL RVVGEDNFLP 310 320 330 340 350 360 SSTNPTMPYT RNTLDEHVDM LMVCHHLDAA IAEDLAFAES RIRKETIAAE DILHDLGAIS 370 380 390 400 410 420 MMSSDSQAMG RVGEVILRTW QTADKMKQQR GALPEDGARN DNHRIKRYVA KYTINPAIAH 430 440 450 460 470 480 GISHDVGSLE VGKWADIVVW KPAFFGVKPA MVLKGGSIAV AAMGDPNASI PTPQPVHYRP 490 500 510 520 530 540 MFGAFGGSLA RSSLTFVSQA AMAAGVRERF GLAKQLSAVR GIRGVRKQHM VHNGYTPRME 550 560 570 IDAQTYTVRA DGQLLTCESA TRLPLAQRYF LF

References

[1]

"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000512 Genomic DNA. Translation: ABM34084.1.
RefSeq	YP_971858.1.
3D structure databases
SMR	A1TSZ6. Positions 2-572.
ModBase	Search...
Protein-protein interaction databases
STRING	A1TSZ6.
Protein family/group databases
MEROPS	M38.982.
Genome annotation databases
GeneID	4667450.
GenomeReviews	Gene locus Aave_3529 in contig CP000512_GR.
KEGG	aav:Aave_3529.
NMPDR	fig|397945.5.peg.3016.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0804.
HOGENOM	HBG357507.
OMA	SHIHFIC.
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

URE1_ACIAC

Accession

Primary (citable) accession number: A1TSZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 6, 2007
Last modified:	February 9, 2010
This is version 29 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)