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Protein
Submitted name:

D-aminoacylase

Gene
N/A
Organism
Alcaligenes faecalis
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi68 – 681Copper; via tele nitrogenCombined sources
Metal bindingi68 – 681Zinc 1; via tele nitrogenCombined sources
Metal bindingi70 – 701Copper; via tele nitrogenCombined sources
Metal bindingi70 – 701Zinc 1; via tele nitrogenCombined sources
Metal bindingi78 – 781Zinc 2; via tele nitrogenCombined sources
Metal bindingi97 – 971CopperCombined sources
Metal bindingi97 – 971Zinc 1Combined sources
Metal bindingi97 – 971Zinc 3Combined sources
Metal bindingi118 – 1181Zinc 2Combined sources
Metal bindingi177 – 1771Zinc 4Combined sources
Metal bindingi202 – 2021Zinc 5Combined sources
Metal bindingi206 – 2061Zinc 5Combined sources
Metal bindingi214 – 2141Zinc 4; via tele nitrogenCombined sources
Metal bindingi221 – 2211Zinc 3; via pros nitrogenCombined sources
Metal bindingi251 – 2511Zinc 3; via tele nitrogenCombined sources
Metal bindingi322 – 3221Zinc 6Combined sources
Metal bindingi326 – 3261Zinc 6Combined sources

GO - Molecular functioni

  1. N-acyl-D-amino-acid deacylase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Keywords - Ligandi

CopperCombined sources, Metal-bindingCombined sources, ZincCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
D-aminoacylaseImported (EC:3.5.1.81Imported)
OrganismiAlcaligenes faecalisImported
Taxonomic identifieri511 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAlcaligenes

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M7JX-ray1.50A1-484[»]
1RJPX-ray1.80A1-484[»]
1RJQX-ray1.80A1-484[»]
1RJRX-ray2.10A1-484[»]
1RK5X-ray1.80A1-484[»]
1RK6X-ray1.43A1-484[»]
1V4YX-ray1.65A1-484[»]
1V51X-ray1.60A1-484[»]
ProteinModelPortaliQ9AGH8.
SMRiQ9AGH8. Positions 8-481.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9AGH8.

Family & Domainsi

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
3.30.1490.130. 1 hit.
InterProiIPR013108. Amidohydro_3.
IPR023100. D-aminoacylase_insert_dom.
IPR012855. D_aminoacylase_C.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamiPF07969. Amidohydro_3. 2 hits.
PF07908. D-aminoacyl_C. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9AGH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPDATPFD YILSGGTVID GTNAPGRLAD VGVRGDRIAA VGDLSASSAR
60 70 80 90 100
RRIDVAGKVV SPGFIDSHTH DDNYLLKHRD MTPKISQGVT TVVTGNCGIS
110 120 130 140 150
LAPLAHANPP APLDLLDEGG SFRFARFSDY LEALRAAPPA VNAACMVGHS
160 170 180 190 200
TLRAAVMPDL RREATADEIQ AMQALADDAL ASGAIGISTG AFYPPAAHAS
210 220 230 240 250
TEEIIEVCRP LITHGGVYAT HMRDEGEHIV QALEETFRIG RELDVPVVIS
260 270 280 290 300
HHKVMGKLNF GRSKETLALI EAAMASQDVS LDAYPYVAGS TMLKQDRVLL
310 320 330 340 350
AGRTLITWCK PYPELSGRDL EEIAAERGKS KYDVVPELQP AGAIYFMMDE
360 370 380 390 400
PDVQRILAFG PTMIGSDGLP HDERPHPRLW GTFPRVLGHY SRDLGLFPLE
410 420 430 440 450
TAVWKMTGLT AAKFGLAERG QVQPGYYADL VVFDPATVAD SATFEHPTER
460 470 480
AAGIHSVYVN GAAVWEDQSF TGQHAGRVLN RAGA
Length:484
Mass (Da):52,001
Last modified:June 1, 2001 - v1
Checksum:i634119A6CB75155E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332548 Genomic DNA. Translation: AAK15530.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332548 Genomic DNA. Translation: AAK15530.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M7JX-ray1.50A1-484[»]
1RJPX-ray1.80A1-484[»]
1RJQX-ray1.80A1-484[»]
1RJRX-ray2.10A1-484[»]
1RK5X-ray1.80A1-484[»]
1RK6X-ray1.43A1-484[»]
1V4YX-ray1.65A1-484[»]
1V51X-ray1.60A1-484[»]
ProteinModelPortaliQ9AGH8.
SMRiQ9AGH8. Positions 8-481.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9AGH8.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
3.30.1490.130. 1 hit.
InterProiIPR013108. Amidohydro_3.
IPR023100. D-aminoacylase_insert_dom.
IPR012855. D_aminoacylase_C.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamiPF07969. Amidohydro_3. 2 hits.
PF07908. D-aminoacyl_C. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Structural-based mutational analysis of D-aminoacylase from Alcaligenes faecalis DA1."
    Hsu C.S., Lai W.L., Chang W.W., Liaw S.H., Tsai Y.C.
    Protein Sci. 11:2545-2550(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism."
    Liaw S.H., Chen S.J., Ko T.P., Hsu C.S., Chen C.J., Wang A.H., Tsai Y.C.
    J. Biol. Chem. 278:4957-4962(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC.
  3. "The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation."
    Lai W.L., Chou L.Y., Ting C.Y., Kirby R., Tsai Y.C., Wang A.H., Liaw S.H.
    J. Biol. Chem. 279:13962-13967(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC.

Entry informationi

Entry nameiQ9AGH8_ALCFA
AccessioniPrimary (citable) accession number: Q9AGH8
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.