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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)DescriptionActionsGraphical viewLength
Binding sitei92Substrate; via amide nitrogenBy similarity1
Active sitei188Nucleophile1 Publication1
Binding sitei188Inhibitor1 Publication1
Binding sitei188Inhibitor (covalent)1 Publication1
Active sitei274Charge relay systemBy similarity1
Active sitei303Charge relay systemBy similarity1

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi88Q → A: Minimal change in catalytic efficiency toward acetate substrates. 1 Publication1
Mutagenesisi92Y → A: Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-228. 1 Publication1
Mutagenesisi102W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication1
Mutagenesisi105W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication1
Mutagenesisi124W → A: Minimal change in catalytic efficiency toward the acetate substrates. 1 Publication1
Mutagenesisi188S → A: Activity abolished towards fluoroscein diacetoxymethyl ether. 1 Publication1
Mutagenesisi213F → A: Reduction in catalytic efficiency towards fluoroscein diacetoxymethyl ether; when associated with A-228. 1 Publication1
Mutagenesisi228P → 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 Publication1
Mutagenesisi276I → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004197661 – 325Cephalosporin-C deacetylaseAdd BLAST325

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

1325
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 11Combined sources4
Helixi24 – 36Combined sources13
Beta strandi43 – 46Combined sources4
Beta strandi52 – 62Combined sources11
Helixi64 – 66Combined sources3
Beta strandi68 – 76Combined sources9
Beta strandi81 – 89Combined sources9
Helixi99 – 102Combined sources4
Helixi104 – 107Combined sources4
Beta strandi111 – 115Combined sources5
Beta strandi123 – 125Combined sources3
Beta strandi134 – 137Combined sources4
Beta strandi142 – 144Combined sources3
Turni145 – 150Combined sources6
Turni152 – 154Combined sources3
Helixi156 – 172Combined sources17
Beta strandi177 – 187Combined sources11
Helixi189 – 200Combined sources12
Beta strandi205 – 211Combined sources7
Beta strandi213 – 215Combined sources3
Helixi217 – 223Combined sources7
Helixi229 – 238Combined sources10
Helixi240 – 242Combined sources3
Helixi243 – 251Combined sources9
Helixi255 – 259Combined sources5
Beta strandi266 – 271Combined sources6
Beta strandi275 – 277Combined sources3
Helixi279 – 288Combined sources10
Beta strandi291 – 298Combined sources8
Turni303 – 306Combined sources4
Helixi307 – 322Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.

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
PDB 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.
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.

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...

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: November 2, 2016
This is version 98 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.