Q3M712 (URE1_ANAVT) 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:	Ava_3618

Organism

Anabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]

Taxonomic identifier

240292 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Protein attributes

Sequence length	568 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 – 568	568	Urease subunit alpha HAMAP MF_01953		PRO_0000239873
Regions
	Domain	131 – 568	438	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)
	Q3M712 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: 32DBF3391914AC2A	FASTA	568	61,125
	10 20 30 40 50 60 MPYRMSRQAY AETYGPTVGD RIRLADTELF IQVEQDFTTY GDEVKFGGGK VIRDGMGQSP 70 80 90 100 110 120 IANADGAVDL VITNALILDW WGIVKADIGI KDGKIFKIGK AGNPYIQDHV DIIIGPGTEA 130 140 150 160 170 180 LAGEGMILTA GGIDTHIHFI CPQQIEVAIA SGITTMIGGG TGPATGTNAT TCTPGPWNMY 190 200 210 220 230 240 RMLQAADAFP MNLGFLGKGN ASQPQGLTEQ IFAGAIGLKL HEDWGTTPAT IDTCLSVADE 250 260 270 280 290 300 YDVQVAIHTD TLNEAGFVED TIAAFKNRAI HTYHTEGAGG GHAPDIIKVC GQANVLPSST 310 320 330 340 350 360 NPTRPYTVNT LDEHLDMLMV CHHLDPAIAE DVAFAESRIR RETIAAEDIL HDLGAFSMIA 370 380 390 400 410 420 SDSQAMGRVG EVIIRTWQTS HKMKVQRGSL AGDGKADNLR AKRYVAKYTI NPAITHGISQ 430 440 450 460 470 480 YVGSVEAGKL ADLCLWRPGF FGVKPEIVIK GGMIAWSQMG DANASIPTPQ PVHMRPMFGS 490 500 510 520 530 540 FAGARNATSL TFVSQAALER DIPQQLGLRK SAVAVSGTRQ LTKQEMKLND ALPHIEVDPE 550 560 TYEVRADGEL LTCEPATVLP MAQRYFLF

References

[1]

"Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000117 Genomic DNA. Translation: ABA23224.1.
RefSeq	YP_324119.1. NC_007413.1.
3D structure databases
ProteinModelPortal	Q3M712.
SMR	Q3M712. Positions 5-568.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3M712.
Protein family/group databases
MEROPS	M38.982.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3679310.
GenomeReviews	Gene locus Ava_3618 in contig CP000117_GR.
KEGG	ava:Ava_3618.
NMPDR	fig|240292.3.peg.4595.
PATRIC	35428401. VBIAnaVar43351_4733.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0804.
HOGENOM	HBG357507.
OMA	TIHAFHT.
PhylomeDB	Q3M712.
ProtClustDB	PRK13207.
Enzyme and pathway databases
BioCyc	AVAR240292:AVA_3618-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. 1 hit.
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_ANAVT

Accession

Primary (citable) accession number: Q3M712

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	October 25, 2005
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program