Q9F4L3 · Q9F4L3_PSEFL
- ProteinBenzaldehyde lyase
- GenebznB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids563 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 26 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 29 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Active site | 50 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 50 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 394 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 395 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 395 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 396 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 419 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 421 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 421 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 448 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 448 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 448 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 448 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 448 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 449 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 449 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 450 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 450 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 453 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 473 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 475 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 475 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 475 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 475 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 475 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 477 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 477 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 479 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 479 | thiamine diphosphate 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 480 | thiamine diphosphate 2 (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | acetolactate synthase complex | |
Molecular Function | acetolactate synthase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | lyase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | thiamine pyrophosphate binding | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | valine biosynthetic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9F4L3
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-121 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: TGGELVVRTLIKAGVEHLFGLHGAHIDTIFQACLDHDVPIIDTRHEAAAGHAAEGYARAGAKLGVALVTAGGGFTNAVTPIANAWLDRTPVLFLTGSGALRDDETNTLQAGIDQVAM | ||||||
Domain | 194-329 | Thiamine pyrophosphate enzyme central | ||||
Sequence: LDQALALLRKAERPVIVLGSEASRTARKTALSAFVAATGVPVFADYEGLSMLSGLPDAMRGGLVQNLYSFAKADAAPDLVLMLGARFGLNTGHGSGQLIPHSAQVIQVDPDACELGRLQGIALGIVADVGGTIEAL | ||||||
Domain | 397-542 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: YLWLSEVMSRVKPGGFLCHGYLGSMGVGFGTALGAQVADLEAGRRTILVTGDGSVGYSIGEFDTLVRKQLPLIVIIMNNQSWGATLHFQQLAVGPNRVTGTRLENGSYHGVAAAFGADGYHVDSVESFSAALAQALAHNRPACINV |
Sequence similarities
Belongs to the TPP enzyme family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length563
- Mass (Da)58,919
- Last updated2001-03-01 v1
- Checksum6511A404C501D126
Keywords
- Technical term