Urease subunit gamma - Enterobacter aerogenes

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P18316 (URE3_ENTAE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

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 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 HAMAP MF_00739.
Sequence similarities	Belongs to the urease gamma subunit family.
Biophysicochemical properties	Kinetic parameters: K_M=2.3 mM for urea Ref.2 Ref.3 Ref.10 Ref.18 V_max=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 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 – 100

100

Urease subunit gamma HAMAP MF_00739

PRO_0000098015

Secondary structure

100

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P18316 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: C5B9E7FAF615C04D
Show »

FASTA

100

11,087

        10         20         30         40         50         60 
MELTPREKDK LLLFTAALVA ERRLARGLKL NYPESVALIS AFIMEGARDG KSVASLMEEG 

        70         80         90        100 
RHVLTREQVM EGVPEMIPDI QVEATFPDGS KLVTVHNPII

« Hide

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: 2211515] [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: 1400317] [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: 8318888] [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: 7909161] [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: 7721685] [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: 7855593] [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: 8808930] [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: 10500143] [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: 11015224] [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: 11594743] [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: 14749331] [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: 7754395] [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: 8718850] [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: 8702515] [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: 9201965] [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: 9558361] [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: 10555581] [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: 10913264] [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	[»]

ProteinModelPortal

P18316.

SMR

P18316. Positions 1-100.

ModBase

Search...

Protein-protein interaction databases

IntAct

P18316. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_00739. Urease_gamma.
[Tree]

InterPro

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

Gene3D

G3DSA:3.30.280.10. Urease_gamma_reg. 1 hit.

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...

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:	December 14, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents