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Q9ZBA9

- DAP_OCHAN

UniProt

Q9ZBA9 - DAP_OCHAN

Protein

D-aminopeptidase

Gene

dap

Organism
Ochrobactrum anthropi
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

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    MSKFDTSALE AFVRHIPQNY KGPGGVVAVV KDGEVVLQHA WGFADLRTRT    50
    PMTLDTRMPI CSVSKQFTCA VLLDAVGEPE LLDDALEAYL DKFEDERPAV 100
    RDLCNNQSGL RDYWALSVLC GADPEGVFLP AQAQSLLRRL KTTHFEPGSH 150
    YSYCNGNFRI LADLIEAHTG RTLVDILSER IFAPAGMKRA ELISDTALFD 200
    ECTGYEGDTV RGFLPATNRI QWMGDAGICA SLNDMIAWEQ FIDATRDDES 250
    GLYRRLSGPQ TFKDGVAAPY GFGLNLHETG GKRLTGHGGA LRGWRCQRWH 300
    CADERLSTIA MFNFEGGASE VAFKLMNIAL GVSSSEVSRV EADSAWFGSW 350
    LDDETGLVLS LEDAGHGRMK ARFGTSPEMM DVVSANEARS AVTTIRRDGE 400
    TIELVRASEN LRLSMKRVKG EAKHDIIGRY HSDELDADLL LVSEGGAIYG 450
    AFEGFLGKSD MYPLYSVGSD VWLLPVQRSM DAPSPGEWKL VFRRDDKGEI 500
    TGLSVGCWLA RGVEYRRVQP 520
    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