DCHI_THEKO
ID DCHI_THEKO Reviewed; 267 AA.
AC Q6F4N1; Q5JDT4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Diacetylchitobiose deacetylase;
DE EC=3.5.1.136 {ECO:0000269|PubMed:15136574};
DE AltName: Full=N-acetylchitobiose deacetylase;
DE AltName: Full=Tk-Dac;
GN Name=dac; OrderedLocusNames=TK1764;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBSTRATE
RP SPECIFICITY, INDUCTION, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15136574; DOI=10.1074/jbc.m314187200;
RA Tanaka T., Fukui T., Fujiwara S., Atomi H., Imanaka T.;
RT "Concerted action of diacetylchitobiose deacetylase and exo-beta-D-
RT glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic
RT archaeon Thermococcus kodakaraensis KOD1.";
RL J. Biol. Chem. 279:30021-30027(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Deacylates the non-reducing end of diacetylchitobiose
CC (GlcNAc2). Can also use N-acetylglucosamine (GlcNAc) and N-
CC acetylchitotriose (GlcNAc3). Probably involved in chitin degradation.
CC {ECO:0000269|PubMed:15136574}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,N'-diacetylchitobiose = acetate + beta-D-glucosaminyl-
CC (1->4)-N-acetyl-D-glucosamine; Xref=Rhea:RHEA:62168,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28681, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:145478; EC=3.5.1.136;
CC Evidence={ECO:0000269|PubMed:15136574};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31.8 mM for GlcNAc2 (at pH 8 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:15136574};
CC KM=98 mM for GlcNAc3 (at pH 8 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:15136574};
CC KM=127 mM for GlcNAc (at pH 8 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:15136574};
CC Vmax=13.3 umol/min/mg enzyme with GlcNAc3 (at pH 8 and at 70 degrees
CC Celsius) {ECO:0000269|PubMed:15136574};
CC Vmax=48.5 umol/min/mg enzyme with GlcNAc2 (at pH 8 and at 70 degrees
CC Celsius) {ECO:0000269|PubMed:15136574};
CC Vmax=133 umol/min/mg enzyme with GlcNAc (at pH 8 and at 70 degrees
CC Celsius) {ECO:0000269|PubMed:15136574};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:15136574};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius. Activity levels at 37 and
CC 100 degrees Celsius are 20% of that observed at the optimal
CC temperature. {ECO:0000269|PubMed:15136574};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000269|PubMed:15136574}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:15136574}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15136574}.
CC -!- INDUCTION: By diacetylchitobiose (GlcNAc2).
CC {ECO:0000269|PubMed:15136574}.
CC -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR EMBL; AB125969; BAD29713.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85953.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F4N1; -.
DR SMR; Q6F4N1; -.
DR IntAct; Q6F4N1; 1.
DR MINT; Q6F4N1; -.
DR STRING; 69014.TK1764; -.
DR EnsemblBacteria; BAD85953; BAD85953; TK1764.
DR KEGG; tko:TK1764; -.
DR PATRIC; fig|69014.16.peg.1720; -.
DR eggNOG; arCOG03460; Archaea.
DR HOGENOM; CLU_049311_3_2_2; -.
DR InParanoid; Q6F4N1; -.
DR OMA; EIVLCNA; -.
DR PhylomeDB; Q6F4N1; -.
DR BioCyc; MetaCyc:MON-16776; -.
DR BRENDA; 3.5.1.105; 5246.
DR BRENDA; 3.5.1.136; 5246.
DR BRENDA; 3.5.1.33; 5246.
DR SABIO-RK; Q6F4N1; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10320; -; 1.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993; PTHR12993; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; SSF102588; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Polysaccharide degradation;
KW Reference proteome.
FT CHAIN 1..267
FT /note="Diacetylchitobiose deacetylase"
FT /id="PRO_0000386548"
SQ SEQUENCE 267 AA; 30302 MW; EE7740F826B43CD7 CRC64;
MVFEEFNNFD EAFSALLSKL DFKINEPFND VKKVLCIEPH PDDCAIGLGG TIKKLTDSGI
DVVYLLLTDG SMGTTDGEVS GHELALRRLE EEKRSAEILG VKKIHALDFG DTELPYTREV
RKEIVTVIRK ERPGIVLMPD PWLPYEGHPD HRHAGFLGIE AVSFAGLPNF NRSDLIAGLD
PHSIQAVGFY YTHKPNYFVD ISDVMEVKLR AVRTHESQFP EDVWELWEPY LRTIALYYGK
MSGHRYAEGI RFVPGIFLHI CPFAHVI
