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Protein
Submitted name:

Hydrolase

Gene
N/A
Organism
Alicyclobacillus acidocaldarius (Bacillus acidocaldarius)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

SABIO-RKQ7SIG1.

Protein family/group databases

ESTHERialiac-est2. Hormone-sensitive_lipase_like.

Names & Taxonomyi

Protein namesi
Submitted name:
HydrolaseImported
OrganismiAlicyclobacillus acidocaldarius (Bacillus acidocaldarius)Imported
Taxonomic identifieri1388 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus

Interactioni

Protein-protein interaction databases

STRINGi1048834.TC41_3218.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVQX-ray2.60A1-310[»]
1QZ3X-ray2.30A1-310[»]
1U4NX-ray2.10A1-310[»]
2HM7X-ray2.00A1-310[»]
ProteinModelPortaliQ7SIG1.
SMRiQ7SIG1. Positions 3-310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIG1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 285209Abhydrolase_3InterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiENOG4105F2M. Bacteria.
COG0657. LUCA.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7SIG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLDPVIQQV LDQLNRMPAP DYKHLSAQQF RSQQSLFPPV KKEPVAEVRE
60 70 80 90 100
FDMDLPGRTL KVRMYRPEGV EPPYPALVYY HGGGWVVGDL ETHDPVCRVL
110 120 130 140 150
AKDGRAVVFS VDYRLAPEHK FPAAVEDAYD ALQWIAERAA DFHLDPARIA
160 170 180 190 200
VGGDSAGGNL AAVTSILAKE RGGPALAFQL LIYPSTGYDP AHPPASIEEN
210 220 230 240 250
AEGYLLTGGM MLWFRDQYLN SLEELTHPWF SPVLYPDLSG LPPAYIATAQ
260 270 280 290 300
YDPLRDVGKL YAEALNKAGV KVEIENFEDL IHGFAQFYSL SPGATKALVR
310
IAEKLRDALA
Length:310
Mass (Da):34,303
Last modified:December 15, 2003 - v1
Checksum:iA7F4C7C8A325014F
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVQX-ray2.60A1-310[»]
1QZ3X-ray2.30A1-310[»]
1U4NX-ray2.10A1-310[»]
2HM7X-ray2.00A1-310[»]
ProteinModelPortaliQ7SIG1.
SMRiQ7SIG1. Positions 3-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1048834.TC41_3218.

Protein family/group databases

ESTHERialiac-est2. Hormone-sensitive_lipase_like.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105F2M. Bacteria.
COG0657. LUCA.

Enzyme and pathway databases

SABIO-RKQ7SIG1.

Miscellaneous databases

EvolutionaryTraceiQ7SIG1.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase."
    De Simone G., Galdiero S., Manco G., Lang D., Rossi M., Pedone C.
    J. Mol. Biol. 303:761-771(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
  2. "A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis."
    De Simone G., Mandrich L., Menchise V., Giordano V., Febbraio F., Rossi M., Pedone C., Manco G.
    J. Biol. Chem. 279:6815-6823(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
  3. "The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family."
    De Simone G., Menchise V., Alterio V., Mandrich L., Rossi M., Manco G., Pedone C.
    J. Mol. Biol. 343:137-146(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
  4. "Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius."
    Mandrich L., Menchise V., Alterio V., De Simone G., Pedone C., Rossi M., Manco G.
    Proteins 71:1721-1731(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).

Entry informationi

Entry nameiQ7SIG1_ALIAC
AccessioniPrimary (citable) accession number: Q7SIG1
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 6, 2016
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.