Q9X758 (ANSME_KLEPN) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 52.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Anaerobic sulfatase-maturating enzyme Short name=AnSME EC=1.1.99.- Alternative name(s): Arylsulfatase-activating protein Ser-type sulfatase-activating enzyme | ||
| Gene names |
| ||
| Organism | Klebsiella pneumoniae | ||
| Taxonomic identifier | 573 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella |
Protein attributes
| Sequence length | 395 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Involved in 'Ser-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of serine ('Ser-72' in the arylsulfatase AtsA) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Ref.3 |
| Cofactor | Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine Probable. May bind at least one other iron-sulfur cluster By similarity. |
| Pathway | |
| Subunit structure | Interacts with AtsA prior to its export to the periplasm. This interaction depends on the presence of AtsA 'Ser-72'. Binding of SAM to AtsB promotes the formation of a ternary AtsA-AtsB-SAM complex. |
| Subcellular location | |
| Sequence similarities | Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 395 | 395 | Anaerobic sulfatase-maturating enzyme | PRO_0000134461 | |||||
Regions | |||||||||
| Region | 83 – 86 | 4 | S-adenosyl-L-methionine binding | ||||||
Sites | |||||||||
| Metal binding | 35 | 1 | Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity | ||||||
| Metal binding | 39 | 1 | Iron-sulfur 1 (4Fe-4S-S-AdoMet) Probable | ||||||
| Metal binding | 42 | 1 | Iron-sulfur 1 (4Fe-4S-S-AdoMet) Probable | ||||||
| Metal binding | 270 | 1 | Iron-sulfur Potential | ||||||
| Metal binding | 276 | 1 | Iron-sulfur Potential | ||||||
| Metal binding | 291 | 1 | Iron-sulfur Potential | ||||||
| Metal binding | 331 | 1 | Iron-sulfur Potential | ||||||
| Metal binding | 334 | 1 | Iron-sulfur Potential | ||||||
| Metal binding | 340 | 1 | Iron-sulfur Potential | ||||||
| Metal binding | 344 | 1 | Iron-sulfur Potential | ||||||
Natural variations | |||||||||
| Natural variant | 24 | 1 | F → L in strain: Isolate 13. | ||||||
| Natural variant | 140 | 1 | G → S in strain: Isolate 13 and Isolate N2. | ||||||
| Natural variant | 177 | 1 | D → G in strain: Isolate 13 and Isolate N2. | ||||||
| Natural variant | 197 | 1 | V → D in strain: Isolate 13 and Isolate N2. | ||||||
| Natural variant | 284 | 1 | S → P in strain: Isolate 13 and Isolate N2. | ||||||
| Natural variant | 297 | 1 | T → A in strain: Isolate 13 and Isolate N2. | ||||||
| Natural variant | 333 | 1 | T → A in strain: Isolate 13. | ||||||
Experimental info | |||||||||
| Mutagenesis | 39 | 1 | C → A: Unable to activate AtsA. No FGly detectable. Binds AtsA with reduced efficiency. Ref.4 | ||||||
| Mutagenesis | 42 | 1 | C → A: Unable to activate AtsA. No FGly detectable. Binds AtsA with reduced efficiency. Ref.4 | ||||||
| Mutagenesis | 83 | 1 | G → A: Drastic reduction in AtsA activity. Abolition of binding to AtsA. No binding to SAM. Ref.4 | ||||||
| Mutagenesis | 84 | 1 | G → A: Drastic reduction in AtsA activity. Abolition of binding to AtsA. No binding to SAM. Ref.4 | ||||||
| Mutagenesis | 85 | 1 | E → A: Drastic reduction in AtsA activity. Abolition of binding to AtsA. No binding to SAM. Ref.4 | ||||||
| Mutagenesis | 86 | 1 | P → G: Binding to AtsA reduced to 60%. No binding to SAM. Still catalytically active. Ref.4 | ||||||
| Mutagenesis | 87 | 1 | L → A: No change in AtsA activity. Ref.4 | ||||||
| Mutagenesis | 88 | 1 | L → A: No change in AtsA activity. Ref.4 | ||||||
| Mutagenesis | 270 | 1 | C → A: Unable to activate AtsA. No FGly detectable. No binding to AtsA. | ||||||
| Mutagenesis | 331 | 1 | C → A: Unable to activate AtsA. No FGly detectable. No binding to AtsA. | ||||||
| Mutagenesis | 334 | 1 | C → A: Unable to activate AtsA. No FGly detectable. No binding to AtsA. | ||||||
Sequences
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References
| [1] | "The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase." Szameit C., Miech C., Balleininger M., Schmidt B., von Figura K., Dierks T. J. Biol. Chem. 274:15375-15381(1999) [PubMed: 10336424] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10031 / DSM 681 / NBRC 3512 / NCIMB 9111 / NCTC 7427. |
| [2] | Coulter-Mackie M.B., Senz J., Siu H. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Isolate 13 and Isolate N2. |
| [3] | "Posttranslational modification of serine to formylglycine in bacterial sulfatases. Recognition of the modification motif by the iron-sulfur protein AtsB." Marquordt C., Fang Q., Will E., Peng J., von Figura K., Dierks T. J. Biol. Chem. 278:2212-2218(2003) [PubMed: 12419807] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-8, FUNCTION, SUBCELLULAR LOCATION, ATSA. |
| [4] | "Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB." Fang Q., Peng J., Dierks T. J. Biol. Chem. 279:14570-14578(2004) [PubMed: 14749327] [Abstract] Cited for: IDENTIFICATION AS A SAM-BINDING PROTEIN, MUTAGENESIS OF CYS-39; CYS-42; GLY-83; GLY-84; GLU-85; PRO-86; LEU-87 AND LEU-88. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ131525 Genomic DNA. Translation: CAB40960.1. AF262989 Genomic DNA. Translation: AAF71374.1. AF262990 Genomic DNA. Translation: AAF71376.1. |
| PIR | T45547. |
3D structure databases | |
| ProteinModelPortal | Q9X758. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR023885. 4Fe4S-binding_SPASM_dom. IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR007197. rSAM. IPR023867. Sulphatase_maturase_rSAM. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| Pfam | PF04055. Radical_SAM. 1 hit. [Graphical view] |
| SMART | SM00729. Elp3. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR04085. RSAM_more_4Fe4S. 1 hit. TIGR03942. Sulfatase_rSAM. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ANSME_KLEPN | ||||||||
| Accession | Primary (citable) accession number: Q9X758 Secondary accession number(s): Q9L4Y3, Q9L4Y5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |