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Q9AGH8 (Q9AGH8_ALCFA) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
EC=3.5.1.81 EMBL AAK15530.1
OrganismAlcaligenes faecalis EMBL AAK15530.1
Taxonomic identifier511 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAlcaligenes

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding681Copper; via tele nitrogen
Metal binding681Zinc 1; via tele nitrogen PDB 1RJR PDB 1M7J PDB 1V4Y PDB 1V51
Metal binding701Copper; via tele nitrogen
Metal binding701Zinc 1; via tele nitrogen PDB 1RJR PDB 1M7J PDB 1V4Y PDB 1V51
Metal binding781Zinc 2; via tele nitrogen PDB 1V51
Metal binding971Copper
Metal binding971Zinc 1 PDB 1RJR PDB 1M7J PDB 1V4Y
Metal binding971Zinc 3 PDB 1RJR PDB 1M7J PDB 1RK6 PDB 1V51 PDB 1RJP PDB 1RK5 PDB 1RJQ
Metal binding1181Zinc 2 PDB 1V51
Metal binding1771Zinc 4 PDB 1V51
Metal binding2021Zinc 5 PDB 1V51
Metal binding2061Zinc 5 PDB 1V51
Metal binding2141Zinc 4; via tele nitrogen PDB 1V51
Metal binding2211Zinc 3; via pros nitrogen PDB 1RJR PDB 1M7J PDB 1RK6 PDB 1V51 PDB 1RJP PDB 1RK5 PDB 1RJQ
Metal binding2511Zinc 3; via tele nitrogen PDB 1RJR PDB 1M7J PDB 1RK6 PDB 1V51 PDB 1RJP PDB 1RK5 PDB 1RJQ
Metal binding3221Zinc 6 PDB 1V51
Metal binding3261Zinc 6 PDB 1V51
Metal binding3671Zinc 1 PDB 1V4Y PDB 1V51

Sequences

Sequence LengthMass (Da)Tools
Q9AGH8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 634119A6CB75155E

FASTA48452,001
        10         20         30         40         50         60 
MSQPDATPFD YILSGGTVID GTNAPGRLAD VGVRGDRIAA VGDLSASSAR RRIDVAGKVV 

        70         80         90        100        110        120 
SPGFIDSHTH DDNYLLKHRD MTPKISQGVT TVVTGNCGIS LAPLAHANPP APLDLLDEGG 

       130        140        150        160        170        180 
SFRFARFSDY LEALRAAPPA VNAACMVGHS TLRAAVMPDL RREATADEIQ AMQALADDAL 

       190        200        210        220        230        240 
ASGAIGISTG AFYPPAAHAS TEEIIEVCRP LITHGGVYAT HMRDEGEHIV QALEETFRIG 

       250        260        270        280        290        300 
RELDVPVVIS HHKVMGKLNF GRSKETLALI EAAMASQDVS LDAYPYVAGS TMLKQDRVLL 

       310        320        330        340        350        360 
AGRTLITWCK PYPELSGRDL EEIAAERGKS KYDVVPELQP AGAIYFMMDE PDVQRILAFG 

       370        380        390        400        410        420 
PTMIGSDGLP HDERPHPRLW GTFPRVLGHY SRDLGLFPLE TAVWKMTGLT AAKFGLAERG 

       430        440        450        460        470        480 
QVQPGYYADL VVFDPATVAD SATFEHPTER AAGIHSVYVN GAAVWEDQSF TGQHAGRVLN 


RAGA 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF332548 Genomic DNA. Translation: AAK15530.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9AGH8.
SMRQ9AGH8. Positions 8-481.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.1490.130. 1 hit.
InterProIPR013108. Amidohydro_3.
IPR023100. D-aminoacylase_insert_dom.
IPR012855. D_aminoacylase_C.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF07969. Amidohydro_3. 2 hits.
PF07908. D-aminoacyl_C. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9AGH8.

Entry information

Entry nameQ9AGH8_ALCFA
AccessionPrimary (citable) accession number: Q9AGH8
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)