P18316 (URE3_ENTAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Urease subunit gamma
EC=3.5.1.5

Alternative name(s):
Urea amidohydrolase subunit gamma

Gene names

Name:

ureA

Organism

Enterobacter aerogenes (Aerobacter aerogenes)

Taxonomic identifier

548 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter

Protein attributes

Sequence length	100 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Urea + H2O = CO2 + 2 NH3. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Enzyme regulation	The apoenzyme can be activated in vitro in the presence of nickel ions and carbon dioxide, which promotes carbamylation of 'Lys-217' of the UreC (alpha) subunit. Ref.6 Ref.7 Ref.8 Ref.9
Pathway	Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. HAMAP-Rule MF_00739
Subunit structure	Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme. The apoenzyme interacts with an accessory complex composed of UreD, UreF and UreG, which is required for the assembly of the nickel containing metallocenter of UreC. The UreE protein may also play a direct role as a metallochaperone in nickel transfer to the urease apoprotein. Ref.4 Ref.5 Ref.7 Ref.8 Ref.11
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the urease gamma subunit family.
Biophysicochemical properties	Kinetic parameters: KM=2.3 mM for urea Ref.2 Ref.3 Ref.10 Ref.18 Vmax=1.9 mmol/min/mg enzyme pH dependence: Optimum pH is 7.75.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	urea catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 100

100

Urease subunit gamma HAMAP-Rule MF_00739

PRO_0000098015

Secondary structure

1

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100

Helix Strand Turn

Details...

Helix

5 – 25

21

Helix

32 – 49

18

Helix

53 – 59

7

Helix

60 – 62

3

Helix

66 – 68

3

Helix

73 – 76

4

Beta strand

78 – 86

9

Beta strand

89 – 97

9

Sequences

	Sequence		Length	Mass (Da)
	P18316 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: C5B9E7FAF615C04D	FASTA	100	11,087
	10 20 30 40 50 60 MELTPREKDK LLLFTAALVA ERRLARGLKL NYPESVALIS AFIMEGARDG KSVASLMEEG 70 80 90 100 RHVLTREQVM EGVPEMIPDI QVEATFPDGS KLVTVHNPII

References

[1]	"Sequence of the Klebsiella aerogenes urease genes and evidence for accessory proteins facilitating nickel incorporation." Mulrooney S.B., Hausinger R.P. J. Bacteriol. 172:5837-5843(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY. Strain: CG253.
[2]	"Site-directed mutagenesis of the active site cysteine in Klebsiella aerogenes urease." Martin P.R., Hausinger R.P. J. Biol. Chem. 267:20024-20027(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"Site-directed mutagenesis of Klebsiella aerogenes urease: identification of histidine residues that appear to function in nickel ligation, substrate binding, and catalysis." Park I.-S., Hausinger R.P. Protein Sci. 2:1034-1041(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly." Park I.-S., Carr M.B., Hausinger R.P. Proc. Natl. Acad. Sci. U.S.A. 91:3233-3237(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREB; UREC AND URED.
[5]	"Evidence for the presence of urease apoprotein complexes containing UreD, UreF, and UreG in cells that are competent for in vivo enzyme activation." Park I.-S., Hausinger R.P. J. Bacteriol. 177:1947-1951(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, INTERACTION WITH UREB; UREC; URED; UREF AND UREG.
[6]	"Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter." Park I.-S., Hausinger R.P. Science 267:1156-1158(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
[7]	"Purification and activation properties of UreD-UreF-urease apoprotein complexes." Moncrief M.B.C., Hausinger R.P. J. Bacteriol. 178:5417-5421(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREB; UREC; URED AND UREF.
[8]	"GTP-dependent activation of urease apoprotein in complex with the UreD, UreF, and UreG accessory proteins." Soriano A., Hausinger R.P. Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH UREB; UREC; URED; UREF AND UREG.
[9]	"UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-urease apoprotein complex." Soriano A., Colpas G.J., Hausinger R.P. Biochemistry 39:12435-12440(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, ACTIVATION OF THE APOPROTEIN BY UREE.
[10]	"Dual effects of ionic strength on Klebsiella aerogenes urease: pH-dependent activation and inhibition." Mulrooney S.B., Zakharian T., Schaller R.A., Hausinger R.P. Arch. Biochem. Biophys. 394:280-282(2001) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[11]	"Chemical cross-linking and mass spectrometric identification of sites of interaction for UreD, UreF, and urease." Chang Z., Kuchar J., Hausinger R.P. J. Biol. Chem. 279:15305-15313(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UREB; UREC; URED AND UREF, MASS SPECTROMETRY.
[12]	"The crystal structure of urease from Klebsiella aerogenes." Jabri E., Carr M.B., Hausinger R.P., Karplus P.A. Science 268:998-1004(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
[13]	"Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants." Jabri E., Karplus P.A. Biochemistry 35:10616-10626(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
[14]	"Characterization of the mononickel metallocenter in H134A mutant urease." Park I.-S., Michel L.O., Pearson M.A., Jabri E., Karplus P.A., Wang S., Dong J., Scott R.A., Koehler B.P., Johnson M.K., Hausinger R.P. J. Biol. Chem. 271:18632-18637(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
[15]	"Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease." Pearson M.A., Michel L.O., Hausinger R.P., Karplus P.A. Biochemistry 36:8164-8172(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND ACETOHYDROXAMIC ACID.
[16]	"Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand." Pearson M.A., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P. Biochemistry 37:6214-6220(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND FORMATE.
[17]	"Characterization of metal-substituted Klebsiella aerogenes urease." Yamaguchi K., Cosper N.J., Staalhandske C., Scott R.A., Pearson M.A., Karplus P.A., Hausinger R.P. J. Biol. Inorg. Chem. 4:468-477(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
[18]	"Kinetic and structural characterization of urease active site variants." Pearson M.A., Park I.-S., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P. Biochemistry 39:8575-8584(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH UREB AND UREC, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M36068 Genomic DNA. Translation: AAA25149.1.

PIR

A36138.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A5K	X-ray	2.20	A	1-100	[»]
1A5L	X-ray	2.20	A	1-100	[»]
1A5M	X-ray	2.00	A	1-100	[»]
1A5N	X-ray	2.40	A	1-100	[»]
1A5O	X-ray	2.50	A	1-100	[»]
1EF2	X-ray	2.50	C	1-100	[»]
1EJR	X-ray	2.00	A	1-100	[»]
1EJS	X-ray	2.00	A	1-100	[»]
1EJT	X-ray	2.00	A	1-100	[»]
1EJU	X-ray	2.00	A	1-100	[»]
1EJV	X-ray	2.40	A	1-100	[»]
1EJW	X-ray	1.90	A	1-100	[»]
1EJX	X-ray	1.60	A	1-100	[»]
1FWA	X-ray	2.00	A	1-100	[»]
1FWB	X-ray	2.00	A	1-100	[»]
1FWC	X-ray	2.00	A	1-100	[»]
1FWD	X-ray	2.00	A	1-100	[»]
1FWE	X-ray	2.00	A	1-100	[»]
1FWF	X-ray	2.00	A	1-100	[»]
1FWG	X-ray	2.00	A	1-100	[»]
1FWH	X-ray	2.00	A	1-100	[»]
1FWI	X-ray	2.00	A	1-100	[»]
1FWJ	X-ray	2.20	A	1-100	[»]
1KRA	X-ray	2.30	A	1-100	[»]
1KRB	X-ray	2.50	A	1-100	[»]
1KRC	X-ray	2.50	A	1-100	[»]
2KAU	X-ray	2.00	A	1-100	[»]
4EP8	X-ray	1.55	A	1-100	[»]
4EPB	X-ray	1.75	A	1-100	[»]
4EPD	X-ray	1.70	A	1-100	[»]
4EPE	X-ray	2.05	A	1-100	[»]

ProteinModelPortal

P18316.

SMR

P18316. Positions 1-100.

ModBase

Search...

Protein-protein interaction databases

IntAct

P18316. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P18316.

UniPathway

UPA00258; UER00370.

Family and domain databases

Gene3D

3.30.280.10. 1 hit.

HAMAP

MF_00739. Urease_gamma.

InterPro

IPR002026. Urease_gamma/gamma-beta_su.
IPR012010. Urease_gamma_su.
[Graphical view]

Pfam

PF00547. Urease_gamma. 1 hit.
[Graphical view]

PIRSF

PIRSF001223. Urease_gamma. 1 hit.

ProDom

PD002319. Urease_gamma_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF54111. Urease_gamma_reg. 1 hit.

TIGRFAMs

TIGR00193. urease_gam. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P18316.

Entry information

Entry name

URE3_ENTAE

Accession

Primary (citable) accession number: P18316

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program