| IED ID | IndEnz0002014189 |
| Enzyme Type ID | protease014189 |
| Protein Name |
Bacterial leucyl aminopeptidase EC 3.4.11.10 |
| Gene Name | |
| Organism | Vibrio proteolyticus (Aeromonas proteolytica) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio proteolyticus (Aeromonas proteolytica) |
| Enzyme Sequence | MKYTKTLLAMVLSATFCQAYAEDKVWISIGADANQTVMKSGAESILPNSVASSGQVWVGQVDVAQLAELSHNMHEEHNRCGGYMVHPSAQSAMAASAMPTTLASFVMPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIASEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDSTIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSNFTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATGDTPTPGNQLEDGVPVTDLSGSRGSNVWYTFELETQKNLQITTSGGYGDLDLYVKFGSKASKQNWDCRPYLSGNNEVCTFNNASPGTYSVMLTGYSNYSGASLKASTF |
| Enzyme Length | 504 |
| Uniprot Accession Number | Q01693 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; |
| DNA Binding | |
| EC Number | 3.4.11.10 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (10); Chain (1); Disulfide bond (1); Helix (12); Metal binding (6); Propeptide (2); Sequence conflict (3); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1569090}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (22) |
| Cross Reference PDB | 1AMP; 1CP6; 1FT7; 1IGB; 1LOK; 1RTQ; 1TXR; 1XRY; 2ANP; 2DEA; 2IQ6; 2NYQ; 2PRQ; 3B35; 3B3C; 3B3S; 3B3T; 3B3V; 3B3W; 3B7I; 3FH4; 3VH9; |
| Mapped Pubmed ID | 12176384; 15274616; 16142900; 16596389; 17238863; 17574677; 18576673; 19233285; 22311113; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,232 |
| Kinetics | |
| Metal Binding | METAL 203; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"; METAL 223; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"; METAL 223; /note="Zinc 2; catalytic"; /evidence="ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"; METAL 258; /note="Zinc 2; catalytic"; /evidence="ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"; METAL 285; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9"; METAL 362; /note="Zinc 2; via tele nitrogen; catalytic"; /evidence="ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.10; |