| IED ID | IndEnz0002002854 |
| Enzyme Type ID | protease002854 |
| Protein Name |
Probable ubiquitin carboxyl-terminal hydrolase creB EC 3.4.19.12 Carbon catabolite repression protein B Deubiquitinating enzyme creB Ubiquitin thioesterase creB Ubiquitin-hydrolyzing enzyme creB Ubiquitin-specific-processing protease creB |
| Gene Name | creB NFIA_103430 |
| Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Enzyme Sequence | MGSFLRSFRHNGGSTAPSVGAVPAKKEPQPPPMTPLEKRLLDMGPIREDGSDKFYGMENYGNTCYCNSILQCLYYSVPFREAVINYPTRTPIESLEAALAKSLRYPNPNAQLEAEAQAEKQKAANAQRPGMPPNPQQKPEDKDSPEYKKKMALQTLPLLETQNNAASYGMSESLFTSLKDIFESVVGSQSRIGIIRPQQFLEVLRRDHEMFRTAMHQDAHEFLNLLLNEVVANVEAEASKQPLMEKSLPAPETADSVDQSSSTGSKTPNTTRWVHELFEGLLTSETQCLTCEKVSQRDEVFLDLSVDLEQHSSVTSCLRKFSAEEMLCERNKFHCDNCGGLQEAEKRMKIKRLPRILALHLKRFKYTEDLQRLQKLFHRVVYPYHLRLFNTTDDAEDPDRLYELYAVVVHIGGGPYHGHYVAIIKTEDRGWLLFDDEMVEPVDKNYVKNFFGDKPGLACAYVLFYQETTLEAVLKEQEQENMDSNLAATDANDTILKQNGFPQSPLAHVHSASQIPSHEDNLRPNGLRRAPTAPQLSTHHEHGDPESTPFSPLSPLSPVPPVPPIPERVATVATPPKNDALAKREEKERKAAEKEKEKAEKLRRKEQGARMKENQRREEAELKAALEMSKASKAEEDRRLSTENGKEKQGGGLSRLKRGSKSLSHRLGKDKETRSVSSDLPPVPIPEHSTLSQSGPTSEQQQQQRQQSPPNHDQPPNSPQPGKPTIREDEQVNHKDSKHERTGHGKWRSFSLRKKSFSILS |
| Enzyme Length | 761 |
| Uniprot Accession Number | A1CW53 |
| Absorption | |
| Active Site | ACT_SITE 64; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 419; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Ubiquitin thioesterase component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Deubiquitinates the creA catabolic repressor and the quinate permease qutD. Plays also a role in response to carbon starvation and the control of extracellular proteases activity (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Coiled coil (1); Compositional bias (6); Domain (1); Erroneous gene model prediction (1); Region (4) |
| Keywords | Coiled coil;Hydrolase;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| 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 | 85,840 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |