Reviewed, UniProtKB/Swiss-Prot Q0RQS0 (URE1_FRAAA)

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:	FRAAL1447

Organism

Frankia alni (strain ACN14a) [Complete proteome] [HAMAP]

Taxonomic identifier

326424 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Frankiaceae › Frankia

Protein attributes

Sequence length	575 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 – 575	575	Urease subunit alpha HAMAP MF_01953		PRO_1000070657
Regions
	Domain	138 – 575	438	Urease
Sites
	Active site	329	1	Proton donor By similarity
	Metal binding	143	1	Nickel 2 By similarity
	Metal binding	145	1	Nickel 2 By similarity
	Metal binding	226	1	Nickel 1; via carbamate group By similarity
	Metal binding	226	1	Nickel 2; via carbamate group By similarity
	Metal binding	255	1	Nickel 1 By similarity
	Metal binding	281	1	Nickel 1 By similarity
	Metal binding	369	1	Nickel 2 By similarity
	Binding site	228	1	Substrate By similarity
Amino acid modifications
	Modified residue	226	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0RQS0-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: CEC03F0B126A9FF2	FASTA	575	60,191
	10 20 30 40 50 60 MSRLDRSRYA SLYGPTVGDR IRLADTDLFI EVTEDRSRGP GLAGSGDEAV FGGGKVIRES 70 80 90 100 110 120 MGQSRATRAQ GAPDLVITGA VVLDHWGVIK ADVGIRDGRI VALGKAGNPD TMDGVHPDLV 130 140 150 160 170 180 IGPGTEIIAG NGKILTAGAV DCHVHLICPQ QVPEALGAGI TTLIGGGTGP AEGTKATTVT 190 200 210 220 230 240 PGSWNLARML SAMDDWPVNI VLLGKGNTVN DESMWEQLRA GAAGFKLHED WGTTPAAIDA 250 260 270 280 290 300 CLRVADAAGV QVALHSDTLN EAGFVEDTLA AIAGRAIHAY HTEGAGGGHA PDIITVAAAA 310 320 330 340 350 360 NVLPSSTNPT RPHTVNTLDE HLDMLMVCHH LNPSVPEDLA FAESRIRPST IAAEDILHDL 370 380 390 400 410 420 GAISMIGSDS QAMGRIGEVV LRTWQTAHVM KRRRGALPGD GPADNARARR YVAKYTICPA 430 440 450 460 470 480 VAHGLDAQIG SVEPGKLADL VVYDPAFFGV RPSLVLKGGF VAWAAMGDAN ASIPTPQPVL 490 500 510 520 530 540 PRPMWGAARG PAAASSLTFV SPAAISDGLP ERLGLATPVV PVEDVRRRGK ADLPENTATP 550 560 570 DIRVDPDTFT VSIDGEAVEA DPVRELPMAQ RYFLF

References

[1]

"Genome characteristics of facultatively symbiotic Frankia sp. strains reflect host range and host plant biogeography." Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., Goltsman E., Huang Y. , Kopp O.R., Labarre L., Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R. Genome Res. 17:7-15(2007) [PubMed: 17151343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CT573213 Genomic DNA. Translation: CAJ60103.1.
RefSeq	YP_711694.1.
3D structure databases
SMR	Q0RQS0. Positions 2-575.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0RQS0.
Genome annotation databases
GeneID	4234638.
GenomeReviews	Gene locus FRAAL1447 in contig CT573213_GR.
KEGG	fal:FRAAL1447.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0804.
HOGENOM	HBG357507.
OMA	SHIHFIC.
Enzyme and pathway databases
BioCyc	FALN326424:FRAAL1447-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. 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_FRAAA

Accession

Primary (citable) accession number: Q0RQS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 5, 2006
Last modified:	February 9, 2010
This is version 33 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)