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Protein

D-aminopeptidase

Gene

dap

Organism
Ochrobactrum anthropi
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
    Active sitei62NucleophileCurated1
    Active sitei65Proton donor/acceptorCurated1
    Binding sitei481Substrate1

    GO - Molecular functioni

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi58M → F: No effect on enzymatic activity. 1 Publication1
    Mutagenesisi61C → S: Alters sensitivity to p-chloromercuribenzoate. 1 Publication1
    Mutagenesisi62S → G: Abolishes enzymatic activity. 1 Publication1
    Mutagenesisi65K → N: Abolishes enzymatic activity. 1 Publication1
    Mutagenesisi69C → S: No effect on enzymatic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00002506962 – 520D-aminopeptidaseAdd BLAST519

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1520
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi7 – 14Combined sources8
    Helixi16 – 19Combined sources4
    Beta strandi22 – 31Combined sources10
    Beta strandi34 – 45Combined sources12
    Turni46 – 49Combined sources4
    Helixi61 – 63Combined sources3
    Helixi64 – 75Combined sources12
    Helixi79 – 82Combined sources4
    Helixi83 – 89Combined sources7
    Turni90 – 92Combined sources3
    Helixi100 – 104Combined sources5
    Helixi113 – 119Combined sources7
    Helixi130 – 138Combined sources9
    Helixi155 – 169Combined sources15
    Helixi173 – 180Combined sources8
    Helixi182 – 185Combined sources4
    Helixi196 – 198Combined sources3
    Beta strandi205 – 208Combined sources4
    Turni209 – 211Combined sources3
    Beta strandi212 – 215Combined sources4
    Beta strandi224 – 226Combined sources3
    Beta strandi228 – 230Combined sources3
    Helixi232 – 244Combined sources13
    Turni245 – 247Combined sources3
    Helixi252 – 256Combined sources5
    Beta strandi269 – 271Combined sources3
    Beta strandi274 – 279Combined sources6
    Beta strandi282 – 291Combined sources10
    Beta strandi294 – 301Combined sources8
    Helixi302 – 304Combined sources3
    Beta strandi306 – 316Combined sources11
    Helixi318 – 330Combined sources13
    Helixi344 – 346Combined sources3
    Beta strandi348 – 351Combined sources4
    Turni353 – 355Combined sources3
    Beta strandi358 – 363Combined sources6
    Beta strandi368 – 372Combined sources5
    Beta strandi374 – 376Combined sources3
    Beta strandi378 – 384Combined sources7
    Beta strandi387 – 389Combined sources3
    Beta strandi394 – 398Combined sources5
    Beta strandi401 – 406Combined sources6
    Helixi407 – 409Combined sources3
    Beta strandi411 – 417Combined sources7
    Beta strandi428 – 432Combined sources5
    Turni433 – 436Combined sources4
    Beta strandi437 – 444Combined sources8
    Beta strandi447 – 454Combined sources8
    Beta strandi465 – 468Combined sources4
    Beta strandi471 – 476Combined sources6
    Beta strandi480 – 483Combined sources4
    Beta strandi486 – 494Combined sources9
    Beta strandi500 – 507Combined sources8
    Beta strandi510 – 517Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EI5X-ray1.90A1-520[»]
    ProteinModelPortaliQ9ZBA9.
    SMRiQ9ZBA9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZBA9.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni477 – 487Important for specificityAdd BLAST11

    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. 1 hit.
    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.
    [Graphical view]
    PfamiPF00144. Beta-lactamase. 1 hit.
    PF07930. DAP_B. 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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M84523 Genomic DNA. Translation: AAA25519.1.
    PIRiA42209.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M84523 Genomic DNA. Translation: AAA25519.1.
    PIRiA42209.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1EI5X-ray1.90A1-520[»]
    ProteinModelPortaliQ9ZBA9.
    SMRiQ9ZBA9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiS12.002.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    SABIO-RKQ9ZBA9.

    Miscellaneous databases

    EvolutionaryTraceiQ9ZBA9.

    Family and domain databases

    Gene3Di2.40.128.50. 2 hits.
    3.40.710.10. 1 hit.
    HAMAPiMF_01960. D_aminopeptidase. 1 hit.
    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.
    [Graphical view]
    PfamiPF00144. Beta-lactamase. 1 hit.
    PF07930. DAP_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF50886. SSF50886. 2 hits.
    SSF56601. SSF56601. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 62 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

    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.