| IED ID | IndEnz0002007984 |
| Enzyme Type ID | protease007984 |
| Protein Name |
Coenzyme PQQ synthesis protein F EC 3.4.24.- Pyrroloquinoline quinone biosynthesis protein F |
| Gene Name | pqqF PA1973 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MDHHAQHHPRSHACVLPNGLRLHLAHDPAASRAAAWLRVAAGSHDEPSAHPGLAHFLEHLSFLGGAAFPGDERLMPWLQVRGGQVNASTLGKTTDYFFEVTAEHLGAGLARLIDMLARPLLDIDAQRREREVLEAEYLARSADEQTLIDAALALGLPAGHPLRRFAAGRRDSLALESDAFQRALREFHAAHYHAGNCQLWLQGPQTLDELERLAQRACADLPGRAPGASPPPPPLLPFACEALALRLPGPPRLVLGFALDALRGADEQTLLAFAELLGDRSPGGLLAALGEQGLGESVALRVVHRDARQALLALTFELFDGSAAAALEAAFFDWLGALRDDAASLLAARRPLLAEPTAPLERLRQRVLGLPAEIRPACLDALRADRCLRLHLDSELDGAEARWSAGFRLSVAPVAAAPPLAAQRHAWRFELPLPPSAAAEGALFLRWRFPGVPARSRFLALRQALRPLCGQARLGGVEMGLEALGEDWSLSLLGPRDRLEAAVRPALARLLAAPPDWRANGERLSSAERRRSATGLPIRQLLDALPGLLGEPLAEVDDWRRTRWDALVMQAAMPDPRWMPGQAAGERLEPLPPRPGRHRRELAVDGESALLLFCPLPTQEVPMEAAWRLLARLHEPAFQRRLRDELQLGYALFCGFREVGARRGLLFAAQSPRACPARLLEHMETFLQRSAEALAQLPARRLAGLRKALADDLRRAPGSFAERARRAWAEHLGGGAGRSRLLAEAALGLSGDDLLAAQARLLEARGGWWVLSSRR |
| Enzyme Length | 775 |
| Uniprot Accession Number | Q9I2D2 |
| Absorption | |
| Active Site | ACT_SITE 58; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. It is thought that this protein is a protease that cleaves peptides bond in a small peptide (gene pqqA), providing the glutamate and tyrosine residues which are necessary for the synthesis of PQQ (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis. |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3) |
| Keywords | Hydrolase;Metal-binding;Metalloprotease;PQQ biosynthesis;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 84,432 |
| Kinetics | |
| Metal Binding | METAL 55; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 59; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 136; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096 |
| Rhea ID | |
| Cross Reference Brenda |