AMPX_VIBPR
ID AMPX_VIBPR Reviewed; 504 AA.
AC Q01693;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Bacterial leucyl aminopeptidase;
DE EC=3.4.11.10;
DE Flags: Precursor;
OS Vibrio proteolyticus (Aeromonas proteolytica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=671;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 107-136 AND 233-405,
RP AND PROTEOLYTIC PROCESSING.
RC STRAIN=ATCC 15338 / DSM 30189 / CCUG 20302 / JCM 21193 / LMG 3772 / NBRC
RC 13287 / NCIMB 1326;
RX PubMed=1627651; DOI=10.1016/0167-4781(92)90037-z;
RA van Heeke G., Denslow S., Watkins J., Wilson K., Wagner F.;
RT "Cloning and nucleotide sequence of the Vibrio proteolyticus aminopeptidase
RT gene.";
RL Biochim. Biophys. Acta 1131:337-340(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-504, SUBCELLULAR LOCATION, AND
RP PROTEOLYTIC PROCESSING.
RX PubMed=1569090; DOI=10.1016/s0021-9258(18)42457-x;
RA Guenet C., Lepage P., Harris B.A.;
RT "Isolation of the leucine aminopeptidase gene from Aeromonas proteolytica.
RT Evidence for an enzyme precursor.";
RL J. Biol. Chem. 267:8390-8395(1992).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=1550363; DOI=10.1016/0003-9861(92)90141-i;
RA Schalk C., Remy J.M., Chevrier B., Moras D., Tarnus C.;
RT "Rapid purification of the Aeromonas proteolytica aminopeptidase:
RT crystallization and preliminary X-ray data.";
RL Arch. Biochem. Biophys. 294:91-97(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 107-397 IN COMPLEX WITH ZINC.
RX PubMed=8087555; DOI=10.1016/s0969-2126(00)00030-7;
RA Chevrier B., Schalk C., D'Orchymont H., Rondeau J.-M., Moras D., Tarnus C.;
RT "Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical
RT member of the co-catalytic zinc enzyme family.";
RL Structure 2:283-290(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 107-397 IN COMPLEX WITH ZINC AND
RP INHIBITOR.
RX PubMed=8647077; DOI=10.1111/j.1432-1033.1996.0393k.x;
RA Chevrier B., D'Orchymont H., Schalk C., Tarnus C., Moras D.;
RT "The structure of the Aeromonas proteolytica aminopeptidase complexed with
RT a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc
RT ions of the co-catalytic unit.";
RL Eur. J. Biochem. 237:393-398(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 107-397 IN COMPLEX WITH ZINC AND
RP INHIBITOR.
RX PubMed=10413478; DOI=10.1021/bi9900572;
RA De Paola C.C., Bennett B., Holz R.C., Ringe D., Petsko G.A.;
RT "1-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a
RT case of arrested development.";
RL Biochemistry 38:9048-9053(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 107-397 IN COMPLEX WITH ZINC AND
RP INHIBITOR.
RX PubMed=11401547; DOI=10.1021/bi0100891;
RA Stamper C., Bennett B., Edwards T., Holz R.C., Ringe D., Petsko G.A.;
RT "Inhibition of the aminopeptidase from Aeromonas proteolytica by L-
RT leucinephosphonic acid. Spectroscopic and crystallographic characterization
RT of the transition state of peptide hydrolysis.";
RL Biochemistry 40:7035-7046(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC but not glutamic or aspartic acids.; EC=3.4.11.10;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547,
CC ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10413478,
CC ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555,
CC ECO:0000269|PubMed:8647077};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1569090}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC {ECO:0000305}.
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DR EMBL; Z11993; CAA78039.1; -; Genomic_DNA.
DR EMBL; M85159; AAA21940.1; -; Genomic_DNA.
DR PIR; S24314; S24314.
DR PDB; 1AMP; X-ray; 1.80 A; A=107-397.
DR PDB; 1CP6; X-ray; 1.90 A; A=107-397.
DR PDB; 1FT7; X-ray; 2.20 A; A=107-397.
DR PDB; 1IGB; X-ray; 2.30 A; A=107-397.
DR PDB; 1LOK; X-ray; 1.20 A; A=107-397.
DR PDB; 1RTQ; X-ray; 0.95 A; A=107-405.
DR PDB; 1TXR; X-ray; 2.00 A; A=107-405.
DR PDB; 1XRY; X-ray; 2.10 A; A=107-405.
DR PDB; 2ANP; X-ray; 1.90 A; A=107-397.
DR PDB; 2DEA; X-ray; 1.24 A; A=107-405.
DR PDB; 2IQ6; X-ray; 2.00 A; A=107-397.
DR PDB; 2NYQ; X-ray; 2.50 A; A=107-405.
DR PDB; 2PRQ; X-ray; 2.15 A; A=107-397.
DR PDB; 3B35; X-ray; 1.10 A; A=107-397.
DR PDB; 3B3C; X-ray; 1.46 A; A=107-397.
DR PDB; 3B3S; X-ray; 1.18 A; A=107-397.
DR PDB; 3B3T; X-ray; 1.17 A; A=107-397.
DR PDB; 3B3V; X-ray; 1.22 A; A=107-397.
DR PDB; 3B3W; X-ray; 1.75 A; A=107-397.
DR PDB; 3B7I; X-ray; 1.75 A; A=107-397.
DR PDB; 3FH4; X-ray; 1.95 A; A=107-405.
DR PDB; 3VH9; X-ray; 1.29 A; A=107-405.
DR PDBsum; 1AMP; -.
DR PDBsum; 1CP6; -.
DR PDBsum; 1FT7; -.
DR PDBsum; 1IGB; -.
DR PDBsum; 1LOK; -.
DR PDBsum; 1RTQ; -.
DR PDBsum; 1TXR; -.
DR PDBsum; 1XRY; -.
DR PDBsum; 2ANP; -.
DR PDBsum; 2DEA; -.
DR PDBsum; 2IQ6; -.
DR PDBsum; 2NYQ; -.
DR PDBsum; 2PRQ; -.
DR PDBsum; 3B35; -.
DR PDBsum; 3B3C; -.
DR PDBsum; 3B3S; -.
DR PDBsum; 3B3T; -.
DR PDBsum; 3B3V; -.
DR PDBsum; 3B3W; -.
DR PDBsum; 3B7I; -.
DR PDBsum; 3FH4; -.
DR PDBsum; 3VH9; -.
DR AlphaFoldDB; Q01693; -.
DR SMR; Q01693; -.
DR BindingDB; Q01693; -.
DR ChEMBL; CHEMBL3750; -.
DR DrugBank; DB02664; 1-Butane Boronic Acid.
DR DrugBank; DB02386; Leucine Phosphonic Acid.
DR DrugBank; DB01980; Para-Iodo-D-Phenylalanine Hydroxamic Acid.
DR DrugBank; DB03424; Ubenimex.
DR DrugCentral; Q01693; -.
DR MEROPS; M28.002; -.
DR BRENDA; 3.4.11.10; 167.
DR SABIO-RK; Q01693; -.
DR EvolutionaryTrace; Q01693; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR012189; Pept_M28E_Ap1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04151; PPC; 1.
DR PIRSF; PIRSF036685; BacLeuNPeptidase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Metal-binding; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..106
FT /evidence="ECO:0000269|PubMed:1569090,
FT ECO:0000269|PubMed:1627651"
FT /id="PRO_0000026849"
FT CHAIN 107..405
FT /note="Bacterial leucyl aminopeptidase"
FT /id="PRO_0000026850"
FT PROPEP 406..504
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:1627651"
FT /id="PRO_0000026851"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10413478,
FT ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555,
FT ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP,
FT ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7,
FT ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK,
FT ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR,
FT ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP,
FT ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6,
FT ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35,
FT ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S,
FT ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V,
FT ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I,
FT ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10413478,
FT ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555,
FT ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP,
FT ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7,
FT ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK,
FT ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR,
FT ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP,
FT ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6,
FT ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35,
FT ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S,
FT ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V,
FT ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I,
FT ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10413478,
FT ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555,
FT ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP,
FT ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7,
FT ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK,
FT ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR,
FT ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP,
FT ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6,
FT ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35,
FT ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S,
FT ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V,
FT ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I,
FT ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10413478,
FT ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555,
FT ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP,
FT ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7,
FT ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK,
FT ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR,
FT ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP,
FT ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6,
FT ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35,
FT ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S,
FT ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V,
FT ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I,
FT ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10413478,
FT ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555,
FT ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP,
FT ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7,
FT ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK,
FT ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR,
FT ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP,
FT ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6,
FT ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35,
FT ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S,
FT ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V,
FT ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I,
FT ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10413478,
FT ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555,
FT ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP,
FT ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7,
FT ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK,
FT ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR,
FT ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP,
FT ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6,
FT ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35,
FT ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S,
FT ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V,
FT ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I,
FT ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"
FT DISULFID 329..333
FT /evidence="ECO:0000269|PubMed:10413478,
FT ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555,
FT ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP,
FT ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7,
FT ECO:0007744|PDB:1IGB"
FT CONFLICT 303..304
FT /note="TD -> DT (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..314
FT /note="TQL -> QT (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 146..163
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2NYQ"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 191..203
FT /evidence="ECO:0007829|PDB:1RTQ"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 225..240
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 262..273
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3B3T"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:1RTQ"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1RTQ"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:1RTQ"
FT HELIX 376..394
FT /evidence="ECO:0007829|PDB:1RTQ"
SQ SEQUENCE 504 AA; 54232 MW; 7B33317EF6153B48 CRC64;
MKYTKTLLAM VLSATFCQAY AEDKVWISIG ADANQTVMKS GAESILPNSV ASSGQVWVGQ
VDVAQLAELS HNMHEEHNRC GGYMVHPSAQ SAMAASAMPT TLASFVMPPI TQQATVTAWL
PQVDASQITG TISSLESFTN RFYTTTSGAQ ASDWIASEWQ ALSASLPNAS VKQVSHSGYN
QKSVVMTITG SEAPDEWIVI GGHLDSTIGS HTNEQSVAPG ADDDASGIAA VTEVIRVLSE
NNFQPKRSIA FMAYAAEEVG LRGSQDLANQ YKSEGKNVVS ALQLDMTNYK GSAQDVVFIT
DYTDSNFTQY LTQLMDEYLP SLTYGFDTCG YACSDHASWH NAGYPAAMPF ESKFNDYNPR
IHTTQDTLAN SDPTGSHAKK FTQLGLAYAI EMGSATGDTP TPGNQLEDGV PVTDLSGSRG
SNVWYTFELE TQKNLQITTS GGYGDLDLYV KFGSKASKQN WDCRPYLSGN NEVCTFNNAS
PGTYSVMLTG YSNYSGASLK ASTF
