GLMA_THEKO
ID GLMA_THEKO Reviewed; 786 AA.
AC Q76HN4; Q5JDU4;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Exo-beta-D-glucosaminidase {ECO:0000303|PubMed:12923090};
DE EC=3.2.1.- {ECO:0000269|PubMed:15136574, ECO:0000269|PubMed:28130448};
DE AltName: Full=GlcNase {ECO:0000303|PubMed:12923090};
GN Name=glmA {ECO:0000303|PubMed:12923090};
GN Synonyms=Tk-Glm {ECO:0000312|EMBL:BAC82164.1};
GN OrderedLocusNames=TK1754 {ECO:0000312|EMBL:BAD85943.1};
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 2-11, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=12923090; DOI=10.1128/jb.185.17.5175-5181.2003;
RA Tanaka T., Fukui T., Atomi H., Imanaka T.;
RT "Characterization of an exo-beta-D-glucosaminidase involved in a novel
RT chitinolytic pathway from the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1.";
RL J. Bacteriol. 185:5175-5181(2003).
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [4] {ECO:0007744|PDB:5GSM}
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) IN COMPLEX WITH BETA-D-GLUCOSAMINE,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ASP-178; GLU-179;
RP GLU-306 AND GLU-347, AND ACTIVE SITE.
RX PubMed=28130448; DOI=10.1074/jbc.m116.766535;
RA Mine S., Watanabe M., Kamachi S., Abe Y., Ueda T.;
RT "The structure of an archaeal beta-glucosaminidase provides insight into
RT glycoside hydrolase evolution.";
RL J. Biol. Chem. 292:4996-5006(2017).
CC -!- FUNCTION: Exo-type enzyme that specifically cleaves the non-reducing
CC terminal glycosidic bond of chitooligosaccharides (PubMed:12923090,
CC PubMed:15136574, PubMed:28130448). Catalyzes the hydrolysis of GlcN-
CC GlcNAc to glucosamine (GlcN) and N-acetylglucosamine (GlcNAc)
CC (PubMed:15136574, PubMed:28130448). Involved in chitin degradation
CC (PubMed:12923090, PubMed:15136574). Can also hydrolyze reduced
CC chitobiose (GlcN2OH) and chitooligosaccharides of various chain lengths
CC (PubMed:12923090). {ECO:0000269|PubMed:12923090,
CC ECO:0000269|PubMed:15136574, ECO:0000269|PubMed:28130448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosaminyl-(1->4)-N-acetyl-D-glucosamine + H2O = D-
CC glucosamine + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:62164,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58723, ChEBI:CHEBI:145478,
CC ChEBI:CHEBI:506227; Evidence={ECO:0000269|PubMed:15136574,
CC ECO:0000269|PubMed:28130448};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.37 mM for GlcN2 {ECO:0000269|PubMed:12923090};
CC KM=0.270 mM for GlcN3 {ECO:0000269|PubMed:12923090};
CC KM=0.295 mM for GlcN4 {ECO:0000269|PubMed:12923090};
CC KM=0.0778 mM for GlcN5 {ECO:0000269|PubMed:12923090};
CC KM=0.365 mM for GlcN6 {ECO:0000269|PubMed:12923090};
CC Vmax=98.7 umol/min/mg enzyme with GlcN2 as substrate
CC {ECO:0000269|PubMed:12923090};
CC Vmax=34.5 umol/min/mg enzyme with GlcN3 as substrate
CC {ECO:0000269|PubMed:12923090};
CC Vmax=41.7 umol/min/mg enzyme with GlcN4 as substrate
CC {ECO:0000269|PubMed:12923090};
CC Vmax=12.0 umol/min/mg enzyme with GlcN5 as substrate
CC {ECO:0000269|PubMed:12923090};
CC Vmax=35.1 umol/min/mg enzyme with GlcN6 as substrate
CC {ECO:0000269|PubMed:12923090};
CC pH dependence:
CC Optimum pH is 6.0 (with reduced chitobiose as substrate).
CC {ECO:0000269|PubMed:12923090};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius (with reduced chitobiose as
CC substrate). {ECO:0000269|PubMed:12923090};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000269|PubMed:12923090, ECO:0000269|PubMed:15136574}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12923090,
CC ECO:0000269|PubMed:28130448}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12923090}.
CC -!- INDUCTION: Induced by GlcNAc(2). Also induced, to a lesser extent, by
CC colloidal chitin. {ECO:0000269|PubMed:12923090}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AB100422; BAC82164.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85943.1; -; Genomic_DNA.
DR RefSeq; WP_011250705.1; NC_006624.1.
DR PDB; 5GSM; X-ray; 1.27 A; A/B=1-786.
DR PDBsum; 5GSM; -.
DR AlphaFoldDB; Q76HN4; -.
DR SMR; Q76HN4; -.
DR STRING; 69014.TK1754; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR EnsemblBacteria; BAD85943; BAD85943; TK1754.
DR GeneID; 3235173; -.
DR KEGG; tko:TK1754; -.
DR PATRIC; fig|69014.16.peg.1710; -.
DR eggNOG; arCOG05856; Archaea.
DR HOGENOM; CLU_395770_0_0_2; -.
DR InParanoid; Q76HN4; -.
DR OMA; WMINEYV; -.
DR OrthoDB; 2265at2157; -.
DR PhylomeDB; Q76HN4; -.
DR BioCyc; MetaCyc:MON-16777; -.
DR BRENDA; 3.2.1.165; 5246.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421; PTHR23421; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12923090"
FT CHAIN 2..786
FT /note="Exo-beta-D-glucosaminidase"
FT /id="PRO_0000449121"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:28130448"
FT ACT_SITE 347
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:28130448"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28130448"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28130448"
FT BINDING 178..179
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28130448"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28130448"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28130448"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28130448"
FT MUTAGEN 178
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28130448"
FT MUTAGEN 179
FT /note="E->Q: Retains less than 3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:28130448"
FT MUTAGEN 306
FT /note="E->Q: Retains 40% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:28130448"
FT MUTAGEN 347
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28130448"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 143..162
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5GSM"
FT TURN 182..187
FT /evidence="ECO:0007829|PDB:5GSM"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 242..270
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 322..339
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:5GSM"
FT TURN 368..372
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:5GSM"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 412..426
FT /evidence="ECO:0007829|PDB:5GSM"
FT TURN 428..432
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 445..453
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 474..480
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 485..489
FT /evidence="ECO:0007829|PDB:5GSM"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 495..499
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 514..525
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 529..534
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 548..553
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 579..586
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 591..600
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 614..622
FT /evidence="ECO:0007829|PDB:5GSM"
FT HELIX 632..643
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 657..663
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 668..673
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 705..714
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 717..730
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 733..737
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 740..750
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 754..765
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 767..775
FT /evidence="ECO:0007829|PDB:5GSM"
FT STRAND 777..785
FT /evidence="ECO:0007829|PDB:5GSM"
SQ SEQUENCE 786 AA; 90232 MW; 74F024EE06C0BD18 CRC64;
MGKVEFSGKR YVIDGEPVTI AGGTLQFFRV PADAWKDRLL KMREAGLNTV DTYVAWNWHE
PEKGSFDFKG ETHPQRNLVG FLELADELGF YVIIRPGPYI CGEWRNGGIP DWLIDEHPEI
LAKGPNGPLP RDIYYPPITY LHPTYLEAVG EWYNAVFPVI RKYLYTNGGP IISVSIDDEP
SYWETIFQPF LTDYNEIITK PGGLWEKWLE QNYTLEDLRR RYKGDFKDYS EIKVPTSFSE
PLPKLIDWHH FKLWMINEYV RWIYERMARE FDVPISILDP YLLQVAWRHF FTYMREHNLK
IHVWTEFWYS FYRSSDFKED KLGHIYYKTG IYRYHVRKAG TPPLSIETQS SLAHTIDPTE
AELLYSILPP LGIPNINYYL FVGGENPEGY ESHNGITWDV YSPVGLDGSE RPHFGVIKAL
SETMTSAEGL ADAELRPKVA VGLYEPYEAL NLWGYEGLEE STDLNEYLLG ERGLFTLLAM
SNTPFDAVDL EDVTLDELLS YDQLWVYSLD FMSREVQDKL VEFVARGGNL VILPMLPRYD
ENLEPYSSLK DFLGVEVERE KARRNPRLIQ FLSVSAEGID RMLVRNTVRG VRGGEPIAFL
GEKPVGAFVR KGGGSAVVLG FRLQYYTSHH DLHRKFVWKL KELQGVREDF EVTNPDMIVL
PMEGKGYAYL AVTNPRGHPI KGRISYRGLE VPVLLDGIEL KRRGTLYLPF GVRKGDVEVA
YATATLVMWE GDVLTFRNHL SGHSEIALKG VESVKVSGGK IVDGSDGEVL RIVIEHPGEY
FEVELL
