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Q9ZBA9

- DAP_OCHAN

UniProt

Q9ZBA9 - DAP_OCHAN

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Protein

D-aminopeptidase

Gene

dap

Organism
Ochrobactrum anthropi
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolyzes N-terminal residues in D-amino acid-containing peptides.

Catalytic activityi

Release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid amides and methyl esters also are hydrolyzed, as is glycine amide.2 Publications

Enzyme regulationi

Inhibited by beta-lactam compounds such as 6-aminopenicillic acid, 7-aminocephalosporanic acid, benzylpenicillin and ampicillin. Inhibited by p-chloromercuribenzoate.1 Publication

Absorptioni

Abs(max)=281 nm1 Publication

Kineticsi

  1. KM=0.65 mM for D-alanine amide (at 30 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei62 – 621NucleophileCurated
Active sitei65 – 651Proton donor/acceptorCurated
Binding sitei481 – 4811Substrate

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Enzyme and pathway databases

SABIO-RKQ9ZBA9.

Protein family/group databases

MEROPSiS12.002.

Names & Taxonomyi

Protein namesi
Recommended name:
D-aminopeptidase (EC:3.4.11.19)
Gene namesi
Name:dap
OrganismiOchrobactrum anthropi
Taxonomic identifieri529 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581M → F: No effect on enzymatic activity. 1 Publication
Mutagenesisi61 – 611C → S: Alters sensitivity to p-chloromercuribenzoate. 1 Publication
Mutagenesisi62 – 621S → G: Abolishes enzymatic activity. 1 Publication
Mutagenesisi65 – 651K → N: Abolishes enzymatic activity. 1 Publication
Mutagenesisi69 – 691C → S: No effect on enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 520519D-aminopeptidasePRO_0000250696Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 148
Helixi16 – 194
Beta strandi22 – 3110
Beta strandi34 – 4512
Turni46 – 494
Helixi61 – 633
Helixi64 – 7512
Helixi79 – 824
Helixi83 – 897
Turni90 – 923
Helixi100 – 1045
Helixi113 – 1197
Helixi130 – 1389
Helixi155 – 16915
Helixi173 – 1808
Helixi182 – 1854
Helixi196 – 1983
Beta strandi205 – 2084
Turni209 – 2113
Beta strandi212 – 2154
Beta strandi224 – 2263
Beta strandi228 – 2303
Helixi232 – 24413
Turni245 – 2473
Helixi252 – 2565
Beta strandi269 – 2713
Beta strandi274 – 2796
Beta strandi282 – 29110
Beta strandi294 – 3018
Helixi302 – 3043
Beta strandi306 – 31611
Helixi318 – 33013
Helixi344 – 3463
Beta strandi348 – 3514
Turni353 – 3553
Beta strandi358 – 3636
Beta strandi368 – 3725
Beta strandi374 – 3763
Beta strandi378 – 3847
Beta strandi387 – 3893
Beta strandi394 – 3985
Beta strandi401 – 4066
Helixi407 – 4093
Beta strandi411 – 4177
Beta strandi428 – 4325
Turni433 – 4364
Beta strandi437 – 4448
Beta strandi447 – 4548
Beta strandi465 – 4684
Beta strandi471 – 4766
Beta strandi480 – 4834
Beta strandi486 – 4949
Beta strandi500 – 5078
Beta strandi510 – 5178

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EI5X-ray1.90A1-520[»]
ProteinModelPortaliQ9ZBA9.
SMRiQ9ZBA9. Positions 3-520.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZBA9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni477 – 48711Important for specificityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S12 family.Curated

Family and domain databases

Gene3Di2.40.128.50. 2 hits.
3.40.710.10. 1 hit.
HAMAPiMF_01960. D_aminopeptidase.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR027279. D_amino_pept/lipop.
IPR009090. D_amino_pept_B/C.
IPR023645. DAP.
IPR012856. DAP_B_dom.
IPR012857. DAP_C_dom.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
PF07930. DAP_B. 1 hit.
PF07932. DAP_C. 1 hit.
[Graphical view]
SUPFAMiSSF50886. SSF50886. 2 hits.
SSF56601. SSF56601. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ZBA9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKFDTSALE AFVRHIPQNY KGPGGVVAVV KDGEVVLQHA WGFADLRTRT
60 70 80 90 100
PMTLDTRMPI CSVSKQFTCA VLLDAVGEPE LLDDALEAYL DKFEDERPAV
110 120 130 140 150
RDLCNNQSGL RDYWALSVLC GADPEGVFLP AQAQSLLRRL KTTHFEPGSH
160 170 180 190 200
YSYCNGNFRI LADLIEAHTG RTLVDILSER IFAPAGMKRA ELISDTALFD
210 220 230 240 250
ECTGYEGDTV RGFLPATNRI QWMGDAGICA SLNDMIAWEQ FIDATRDDES
260 270 280 290 300
GLYRRLSGPQ TFKDGVAAPY GFGLNLHETG GKRLTGHGGA LRGWRCQRWH
310 320 330 340 350
CADERLSTIA MFNFEGGASE VAFKLMNIAL GVSSSEVSRV EADSAWFGSW
360 370 380 390 400
LDDETGLVLS LEDAGHGRMK ARFGTSPEMM DVVSANEARS AVTTIRRDGE
410 420 430 440 450
TIELVRASEN LRLSMKRVKG EAKHDIIGRY HSDELDADLL LVSEGGAIYG
460 470 480 490 500
AFEGFLGKSD MYPLYSVGSD VWLLPVQRSM DAPSPGEWKL VFRRDDKGEI
510 520
TGLSVGCWLA RGVEYRRVQP
Length:520
Mass (Da):57,392
Last modified:January 23, 2007 - v3
Checksum:iCB364A8061DFBF4A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84523 Genomic DNA. Translation: AAA25519.1.
PIRiA42209.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84523 Genomic DNA. Translation: AAA25519.1 .
PIRi A42209.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EI5 X-ray 1.90 A 1-520 [» ]
ProteinModelPortali Q9ZBA9.
SMRi Q9ZBA9. Positions 3-520.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S12.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK Q9ZBA9.

Miscellaneous databases

EvolutionaryTracei Q9ZBA9.

Family and domain databases

Gene3Di 2.40.128.50. 2 hits.
3.40.710.10. 1 hit.
HAMAPi MF_01960. D_aminopeptidase.
InterProi IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR027279. D_amino_pept/lipop.
IPR009090. D_amino_pept_B/C.
IPR023645. DAP.
IPR012856. DAP_B_dom.
IPR012857. DAP_C_dom.
[Graphical view ]
Pfami PF00144. Beta-lactamase. 1 hit.
PF07930. DAP_B. 1 hit.
PF07932. DAP_C. 1 hit.
[Graphical view ]
SUPFAMi SSF50886. SSF50886. 2 hits.
SSF56601. SSF56601. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Structural similarity of D-aminopeptidase carboxypeptidase DD and beta-lactamases."
    Asano Y., Kato Y., Yamada A., Kondo K.
    Biochemistry 31:2316-2328(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF MET-58; CYS-61; SER-62; LYS-65 AND CYS-69, ENZYME REGULATION.
    Strain: ATCC 49237 / SCRC C1-38.
  2. "Properties of a novel D-stereospecific aminopeptidase from Ochrobactrum anthropi."
    Asano Y., Nakazawa A., Kato Y., Kondo K.
    J. Biol. Chem. 264:14233-14239(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 49237 / SCRC C1-38.
  3. "Specificity inversion of Ochrobactrum anthropi D-aminopeptidase to a D,D-carboxypeptidase with new penicillin binding activity by directed mutagenesis."
    Delmarcelle M., Boursoit M.-C., Filee P., Baurin S.L., Frere J.-M., Joris B.
    Protein Sci. 14:2296-2303(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  4. "Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family."
    Bompard-Gilles C., Remaut H., Villeret V., Prange T., Fanuel L., Delmarcelle M., Joris B., Frere J.-M., Van Beeumen J.
    Structure 8:971-980(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-520, PROBABLE ACTIVE SITE.

Entry informationi

Entry nameiDAP_OCHAN
AccessioniPrimary (citable) accession number: Q9ZBA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 55 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3