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Protein

Cephalosporin-C deacetylase

Gene

axeA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Esterase that removes acetyl groups from a number of O-acetylated small substrates, such as acetylated xylose, short xylo-oligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan, 4-methylumbelliferyl acetate or alpha-naphthyl acetate. Able to catalyze rapid hydrolysis of a range of substrates preferably with acetate groups, independent of the alcohol moiety. Exhibits a narrow selectivity for short chain acyl esters (C2-C3). Displays broad substrate specificity by hydrolyzing acetate at 2, 3, and 4 positions of 4-nitrophenyl-beta-D-xylopyranoside (pNP-Xyl) with similar efficiency. Cannot cleave amide linkages.3 Publications

Catalytic activityi

Deacetylation of xylans and xylo-oligosaccharides.2 Publications
Cephalosporin C + H2O = deacetylcephalosporin C + acetate.2 Publications

Enzyme regulationi

Activity stimulated by up to 40% in the presence of divalent cations such as BaCl2, CaCl2, MgCl2 and MnCl2 at 3 mM concentration, but inhibited by 82-85% in the presence of CdCl2 and ZnCl2 at 3 mM concentration.1 Publication

Kineticsi

  1. KM=0.12 mM for p-nitrophenyl-acetate3 Publications
  2. KM=6.05 mM for glucose penta-acetate3 Publications
  3. KM=4.18 mM for cephalosporin-C3 Publications
  4. KM=20.8 mM for 7-aminocephalosporonic acid (7-ACA)3 Publications
  5. KM=760 µM for p-nitrophenyl acetate3 Publications
  6. KM=3.7 µM for fluoroscein di(acetoxymethyl) ether3 Publications
  7. KM=0.97 µM for fluoroscein dipropyloxymethyl ether3 Publications
  8. KM=0.41 µM for fluoroscein dibutyloxymethyl ether3 Publications
  9. KM=1.0 µM for fluoroscein divaleryloxymethyl ether3 Publications
  10. KM=2.6 µM for fluoroscein dicaproyloxymethyl ether3 Publications
  11. KM=0.51 µM for fluoroscein dimethacryloxymethyl ether3 Publications
  12. KM=0.96 µM for fluoroscein dicyclobutylcarboxymethyl ether3 Publications
  13. KM=0.54 µM for fluoroscein dimethylcyclopropanecarboxymethyl ether3 Publications
  14. KM=0.185 mM for p-nitrophenyl-acetate3 Publications
  15. KM=0.137 mM for p-nitrophenyl-propionate3 Publications
  16. KM=3.6 mM for 2-O-acetyl-pNP-Xyl3 Publications
  17. KM=4.2 mM for 3-O-acetyl-pNP-Xyl3 Publications
  18. KM=4.0 mM for 4-O-acetyl-pNP-Xyl3 Publications
  1. Vmax=113.5 µmol/min/mg enzyme with pNP-acetate as substrate3 Publications
  2. Vmax=366.8 µmol/min/mg enzyme with glucose penta-acetate as substrate3 Publications
  3. Vmax=19.2 µmol/min/mg enzyme with cephalosporin-C as substrate3 Publications

pH dependencei

Optimum pH is 6.5. Half-maximal activity between pH 5.0-7.5.3 Publications

Temperature dependencei

Optimum temperature is 90 degrees Celsius. Activity drops sharply above 90 degrees Celsius. Stable up to 100-104 degrees Celsius.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Substrate; via amide nitrogenBy similarity
Active sitei188 – 1881Nucleophile1 Publication
Binding sitei188 – 1881Inhibitor1 Publication
Binding sitei188 – 1881Inhibitor (covalent)1 Publication
Active sitei274 – 2741Charge relay systemBy similarity
Active sitei303 – 3031Charge relay systemBy similarity

GO - Molecular functioni

  • acetylxylan esterase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • cephalosporin-C deacetylase activity Source: UniProtKB
  • hydrolase activity Source: UniProtKB

GO - Biological processi

  • cellulose catabolic process Source: UniProtKB-KW
  • metabolic process Source: UniProtKB
  • polysaccharide metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-77-MONOMER.

Protein family/group databases

ESTHERithema-TM0077. Acetyl-esterase_deacetylase.

Names & Taxonomyi

Protein namesi
Recommended name:
Cephalosporin-C deacetylaseCurated (EC:3.1.1.412 Publications)
Alternative name(s):
Acetylxylan esterase (EC:3.1.1.721 Publication)
Gene namesi
Name:axeA1 Publication
Ordered Locus Names:TM_0077
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi88 – 881Q → A: Minimal change in catalytic efficiency toward acetate substrates. 1 Publication
Mutagenesisi92 – 921Y → A: Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-228. 1 Publication
Mutagenesisi102 – 1021W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication
Mutagenesisi105 – 1051W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication
Mutagenesisi124 – 1241W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication
Mutagenesisi188 – 1881S → A: Activity abolished towards fluoroscein diacetoxymethyl ether. 1 Publication
Mutagenesisi213 – 2131F → A: Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-228. 1 Publication
Mutagenesisi228 – 2281P → A: Reduces catalytic activity by 33-fold against fluoroscein diacetoxymethyl ether; 8-fold decrease in activity against dimethacryloxymethyl ether; 4-fold increase in catalytic efficiency toward dicyclobutylcarboxymethyl ether. Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-92; A-213 or A-276. 1 Publication
Mutagenesisi276 – 2761I → A: Greater than 10-fold reduction in catalytic efficiency toward the acetate substrates. Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-228. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Cephalosporin-C deacetylasePRO_0000419766Add
BLAST

Interactioni

Subunit structurei

Homohexamer, formed by a trimer of dimers. Also exists as a homodimer.2 Publications

Protein-protein interaction databases

STRINGi243274.TM0077.

Structurei

Secondary structure

1
325
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114Combined sources
Helixi24 – 3613Combined sources
Beta strandi43 – 464Combined sources
Beta strandi52 – 6211Combined sources
Helixi64 – 663Combined sources
Beta strandi68 – 769Combined sources
Beta strandi81 – 899Combined sources
Helixi99 – 1024Combined sources
Helixi104 – 1074Combined sources
Beta strandi111 – 1155Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi142 – 1443Combined sources
Turni145 – 1506Combined sources
Turni152 – 1543Combined sources
Helixi156 – 17217Combined sources
Beta strandi177 – 18711Combined sources
Helixi189 – 20012Combined sources
Beta strandi205 – 2117Combined sources
Helixi217 – 2237Combined sources
Helixi229 – 23810Combined sources
Helixi243 – 2519Combined sources
Helixi255 – 2595Combined sources
Beta strandi266 – 2716Combined sources
Beta strandi275 – 2773Combined sources
Helixi279 – 28810Combined sources
Beta strandi291 – 2988Combined sources
Turni303 – 3064Combined sources
Helixi307 – 32216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VLQX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L1-325[»]
3M81X-ray2.50A/B/C/D/E/F1-325[»]
3M82X-ray2.40A/B/C/D/E/F1-325[»]
3M83X-ray2.12A/B/C/D/E/F1-325[»]
5FDFX-ray1.76A/B/C/D/E/F1-325[»]
5HFNX-ray2.75A/B/C/D/E/F1-325[»]
ProteinModelPortaliQ9WXT2.
SMRiQ9WXT2. Positions 2-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WXT2.

Family & Domainsi

Sequence similaritiesi

Belongs to the carbohydrate esterase 7 family.Sequence analysis

Phylogenomic databases

eggNOGiENOG4105I82. Bacteria.
COG3458. LUCA.
InParanoidiQ9WXT2.
KOiK01060.
OMAiNWALHGY.
OrthoDBiEOG6CZQPN.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR008391. AXE1_dom.
[Graphical view]
PfamiPF05448. AXE1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9WXT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFFDLPLEE LKKYRPERYE EKDFDEFWEE TLAESEKFPL DPVFERMESH
60 70 80 90 100
LKTVEAYDVT FSGYRGQRIK GWLLVPKLEE EKLPCVVQYI GYNGGRGFPH
110 120 130 140 150
DWLFWPSMGY ICFVMDTRGQ GSGWLKGDTP DYPEGPVDPQ YPGFMTRGIL
160 170 180 190 200
DPRTYYYRRV FTDAVRAVEA AASFPQVDQE RIVIAGGSQG GGIALAVSAL
210 220 230 240 250
SKKAKALLCD VPFLCHFRRA VQLVDTHPYA EITNFLKTHR DKEEIVFRTL
260 270 280 290 300
SYFDGVNFAA RAKIPALFSV GLMDNICPPS TVFAAYNYYA GPKEIRIYPY
310 320
NNHEGGGSFQ AVEQVKFLKK LFEKG
Length:325
Mass (Da):37,156
Last modified:November 1, 1999 - v1
Checksum:iAF2879D86680A3C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35171.1.
PIRiE72421.
RefSeqiNP_227893.1. NC_000853.1.
WP_004082599.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35171; AAD35171; TM_0077.
GeneIDi896903.
KEGGitma:TM0077.
PATRICi23934994. VBITheMar51294_0075.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35171.1.
PIRiE72421.
RefSeqiNP_227893.1. NC_000853.1.
WP_004082599.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VLQX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L1-325[»]
3M81X-ray2.50A/B/C/D/E/F1-325[»]
3M82X-ray2.40A/B/C/D/E/F1-325[»]
3M83X-ray2.12A/B/C/D/E/F1-325[»]
5FDFX-ray1.76A/B/C/D/E/F1-325[»]
5HFNX-ray2.75A/B/C/D/E/F1-325[»]
ProteinModelPortaliQ9WXT2.
SMRiQ9WXT2. Positions 2-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0077.

Protein family/group databases

ESTHERithema-TM0077. Acetyl-esterase_deacetylase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35171; AAD35171; TM_0077.
GeneIDi896903.
KEGGitma:TM0077.
PATRICi23934994. VBITheMar51294_0075.

Phylogenomic databases

eggNOGiENOG4105I82. Bacteria.
COG3458. LUCA.
InParanoidiQ9WXT2.
KOiK01060.
OMAiNWALHGY.
OrthoDBiEOG6CZQPN.

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-77-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9WXT2.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR008391. AXE1_dom.
[Graphical view]
PfamiPF05448. AXE1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 100991 Publication.
  3. "The structural basis for the narrow substrate specificity of an acetyl esterase from Thermotoga maritima."
    Hedge M.K., Gehring A.M., Adkins C.T., Weston L.A., Lavis L.D., Johnson R.J.
    Biochim. Biophys. Acta 1824:1024-1030(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-88; TYR-92; TRP-102; TRP-105; TRP-124; SER-188; PHE-213; PRO-228 AND ILE-276.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH PMSF AND DIETHYL PHOSPHONATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 100991 Publication.

Entry informationi

Entry nameiCAH_THEMA
AccessioniPrimary (citable) accession number: Q9WXT2
Secondary accession number(s): G4FGZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.