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Q01693

- AMPX_VIBPR

UniProt

Q01693 - AMPX_VIBPR

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Protein

Bacterial leucyl aminopeptidase

Gene
N/A
Organism
Vibrio proteolyticus (Aeromonas proteolytica)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi203 – 2031Zinc 1
Metal bindingi223 – 2231Zinc 1
Metal bindingi223 – 2231Zinc 2; catalytic
Metal bindingi258 – 2581Zinc 2; catalytic
Metal bindingi285 – 2851Zinc 1
Metal bindingi362 – 3621Zinc 2; catalytic

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKQ01693.

Protein family/group databases

MEROPSiM28.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Bacterial leucyl aminopeptidase (EC:3.4.11.10)
OrganismiVibrio proteolyticus (Aeromonas proteolytica)
Taxonomic identifieri671 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 10685Sequence AnalysisPRO_0000026849Add
BLAST
Chaini107 – 405299Bacterial leucyl aminopeptidasePRO_0000026850Add
BLAST
Propeptidei406 – 50499Removed in mature formSequence AnalysisPRO_0000026851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi329 ↔ 333

Keywords - PTMi

Disulfide bond, Zymogen

Miscellaneous databases

PMAP-CutDBQ01693.

Interactioni

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi113 – 1197
Helixi120 – 1223
Helixi125 – 13612
Helixi146 – 16318
Beta strandi164 – 1663
Beta strandi169 – 1768
Beta strandi179 – 18810
Beta strandi191 – 20313
Turni221 – 2244
Helixi225 – 24016
Beta strandi246 – 25510
Helixi257 – 2593
Helixi262 – 27312
Beta strandi277 – 2837
Beta strandi292 – 2998
Beta strandi301 – 3033
Helixi305 – 31814
Beta strandi324 – 3274
Helixi336 – 3416
Beta strandi349 – 3524
Helixi354 – 3563
Turni359 – 3624
Helixi368 – 3703
Helixi376 – 39419

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMPX-ray1.80A107-397[»]
1CP6X-ray1.90A107-397[»]
1FT7X-ray2.20A107-397[»]
1IGBX-ray2.30A107-397[»]
1LOKX-ray1.20A107-397[»]
1RTQX-ray0.95A107-405[»]
1TXRX-ray2.00A107-405[»]
1XRYX-ray2.10A107-405[»]
2ANPX-ray1.90A107-397[»]
2DEAX-ray1.24A107-405[»]
2IQ6X-ray2.00A107-397[»]
2NYQX-ray2.50A107-405[»]
2PRQX-ray2.15A107-397[»]
3B35X-ray1.10A107-397[»]
3B3CX-ray1.46A107-397[»]
3B3SX-ray1.18A107-397[»]
3B3TX-ray1.17A107-397[»]
3B3VX-ray1.22A107-397[»]
3B3WX-ray1.75A107-397[»]
3B7IX-ray1.75A107-397[»]
3FH4X-ray1.95A107-405[»]
3VH9X-ray1.29A107-405[»]
ProteinModelPortaliQ01693.
SMRiQ01693. Positions 107-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01693.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M28 family. M28E subfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR012189. Pept_M28E_Ap1.
IPR007280. Peptidase_C_arc/bac.
IPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PIRSFiPIRSF036685. BacLeuNPeptidase. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q01693 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKYTKTLLAM VLSATFCQAY AEDKVWISIG ADANQTVMKS GAESILPNSV
60 70 80 90 100
ASSGQVWVGQ VDVAQLAELS HNMHEEHNRC GGYMVHPSAQ SAMAASAMPT
110 120 130 140 150
TLASFVMPPI TQQATVTAWL PQVDASQITG TISSLESFTN RFYTTTSGAQ
160 170 180 190 200
ASDWIASEWQ ALSASLPNAS VKQVSHSGYN QKSVVMTITG SEAPDEWIVI
210 220 230 240 250
GGHLDSTIGS HTNEQSVAPG ADDDASGIAA VTEVIRVLSE NNFQPKRSIA
260 270 280 290 300
FMAYAAEEVG LRGSQDLANQ YKSEGKNVVS ALQLDMTNYK GSAQDVVFIT
310 320 330 340 350
DYTDSNFTQY LTQLMDEYLP SLTYGFDTCG YACSDHASWH NAGYPAAMPF
360 370 380 390 400
ESKFNDYNPR IHTTQDTLAN SDPTGSHAKK FTQLGLAYAI EMGSATGDTP
410 420 430 440 450
TPGNQLEDGV PVTDLSGSRG SNVWYTFELE TQKNLQITTS GGYGDLDLYV
460 470 480 490 500
KFGSKASKQN WDCRPYLSGN NEVCTFNNAS PGTYSVMLTG YSNYSGASLK

ASTF
Length:504
Mass (Da):54,232
Last modified:July 1, 1993 - v1
Checksum:i7B33317EF6153B48
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3042TD → DT AA sequence (PubMed:1627651)Curated
Sequence conflicti306 – 3061N → D AA sequence (PubMed:1627651)Curated
Sequence conflicti312 – 3143TQL → QT AA sequence (PubMed:1627651)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11993 Genomic DNA. Translation: CAA78039.1.
M85159 Genomic DNA. Translation: AAA21940.1.
PIRiS24314.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11993 Genomic DNA. Translation: CAA78039.1 .
M85159 Genomic DNA. Translation: AAA21940.1 .
PIRi S24314.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AMP X-ray 1.80 A 107-397 [» ]
1CP6 X-ray 1.90 A 107-397 [» ]
1FT7 X-ray 2.20 A 107-397 [» ]
1IGB X-ray 2.30 A 107-397 [» ]
1LOK X-ray 1.20 A 107-397 [» ]
1RTQ X-ray 0.95 A 107-405 [» ]
1TXR X-ray 2.00 A 107-405 [» ]
1XRY X-ray 2.10 A 107-405 [» ]
2ANP X-ray 1.90 A 107-397 [» ]
2DEA X-ray 1.24 A 107-405 [» ]
2IQ6 X-ray 2.00 A 107-397 [» ]
2NYQ X-ray 2.50 A 107-405 [» ]
2PRQ X-ray 2.15 A 107-397 [» ]
3B35 X-ray 1.10 A 107-397 [» ]
3B3C X-ray 1.46 A 107-397 [» ]
3B3S X-ray 1.18 A 107-397 [» ]
3B3T X-ray 1.17 A 107-397 [» ]
3B3V X-ray 1.22 A 107-397 [» ]
3B3W X-ray 1.75 A 107-397 [» ]
3B7I X-ray 1.75 A 107-397 [» ]
3FH4 X-ray 1.95 A 107-405 [» ]
3VH9 X-ray 1.29 A 107-405 [» ]
ProteinModelPortali Q01693.
SMRi Q01693. Positions 107-397.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q01693.
ChEMBLi CHEMBL3750.

Protein family/group databases

MEROPSi M28.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK Q01693.

Miscellaneous databases

EvolutionaryTracei Q01693.
PMAP-CutDB Q01693.

Family and domain databases

InterProi IPR012189. Pept_M28E_Ap1.
IPR007280. Peptidase_C_arc/bac.
IPR007484. Peptidase_M28.
[Graphical view ]
Pfami PF04389. Peptidase_M28. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view ]
PIRSFi PIRSF036685. BacLeuNPeptidase. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Cloning and nucleotide sequence of the Vibrio proteolyticus aminopeptidase gene."
    van Heeke G., Denslow S., Watkins J., Wilson K., Wagner F.
    Biochim. Biophys. Acta 1131:337-340(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 107-136 AND 233-405.
    Strain: ATCC 15338 / DSM 30189 / JCM 21193 / LMG 3772 / NBRC 13287 / NCIMB 1326.
  2. "Isolation of the leucine aminopeptidase gene from Aeromonas proteolytica. Evidence for an enzyme precursor."
    Guenet C., Lepage P., Harris B.A.
    J. Biol. Chem. 267:8390-8395(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-504.
  3. "Rapid purification of the Aeromonas proteolytica aminopeptidase: crystallization and preliminary X-ray data."
    Schalk C., Remy J.M., Chevrier B., Moras D., Tarnus C.
    Arch. Biochem. Biophys. 294:91-97(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, CRYSTALLIZATION.
  4. "Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family."
    Chevrier B., Schalk C., D'Orchymont H., Rondeau J.-M., Moras D., Tarnus C.
    Structure 2:283-290(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 107-396.
  5. "The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit."
    Chevrier B., D'Orchymont H., Schalk C., Tarnus C., Moras D.
    Eur. J. Biochem. 237:393-398(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  6. "1-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development."
    De Paola C.C., Bennett B., Holz R.C., Ringe D., Petsko G.A.
    Biochemistry 38:9048-9053(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF INHIBITOR COMPLEX.
  7. "Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis."
    Stamper C., Bennett B., Edwards T., Holz R.C., Ringe D., Petsko G.A.
    Biochemistry 40:7035-7046(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF INHIBITOR COMPLEX.

Entry informationi

Entry nameiAMPX_VIBPR
AccessioniPrimary (citable) accession number: Q01693
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 103 of the entry and version 1 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