GLMA_PYRHO
ID GLMA_PYRHO Reviewed; 778 AA.
AC O58247;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Exo-beta-D-glucosaminidase {ECO:0000303|PubMed:16912928};
DE EC=3.2.1.- {ECO:0000269|PubMed:28130448};
DE AltName: Full=GlcNase {ECO:0000303|PubMed:16912928};
GN Name=glmA {ECO:0000303|PubMed:28130448};
GN OrderedLocusNames=PH0511 {ECO:0000312|EMBL:BAA29599.1};
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16912928; DOI=10.1007/s10529-006-9137-0;
RA Liu B., Li Z., Hong Y., Ni J., Sheng D., Shen Y.;
RT "Cloning, expression and characterization of a thermostable exo-beta-D-
RT glucosaminidase from the hyperthermophilic archaeon Pyrococcus
RT horikoshii.";
RL Biotechnol. Lett. 28:1655-1660(2006).
RN [3] {ECO:0007744|PDB:5GSL}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND MUTAGENESIS OF ASP-180; GLU-181; GLU-308 AND GLU-349.
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:16912928,
CC PubMed:28130448). Catalyzes the hydrolysis of GlcN-GlcNAc to
CC glucosamine (GlcN) and N-acetylglucosamine (GlcNAc) (PubMed:28130448).
CC Involved in chitin degradation (PubMed:16912928). Can also hydrolyze
CC chitosan and chitooligosaccharides of various chain lengths
CC (PubMed:16912928). {ECO:0000269|PubMed:16912928,
CC 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:28130448};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:16912928};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius.
CC {ECO:0000269|PubMed:16912928};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000269|PubMed:16912928}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16912928,
CC ECO:0000269|PubMed:28130448}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q76HN4}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; BA000001; BAA29599.1; -; Genomic_DNA.
DR PIR; B71164; B71164.
DR PDB; 5GSL; X-ray; 2.60 A; A/B=1-778.
DR PDBsum; 5GSL; -.
DR AlphaFoldDB; O58247; -.
DR SMR; O58247; -.
DR STRING; 70601.3256916; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR EnsemblBacteria; BAA29599; BAA29599; BAA29599.
DR KEGG; pho:PH0511; -.
DR eggNOG; arCOG05856; Archaea.
DR OMA; WMINEYV; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:InterPro.
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; Glycosidase; Hydrolase.
FT CHAIN 1..778
FT /note="Exo-beta-D-glucosaminidase"
FT /id="PRO_0000449120"
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q76HN4"
FT ACT_SITE 349
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q76HN4"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q76HN4"
FT BINDING 104..105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q76HN4"
FT BINDING 180..181
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q76HN4"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q76HN4"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q76HN4"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q76HN4"
FT MUTAGEN 180
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28130448"
FT MUTAGEN 181
FT /note="E->Q: Retains 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:28130448"
FT MUTAGEN 308
FT /note="E->Q: Retains 15% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:28130448"
FT MUTAGEN 349
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28130448"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 145..164
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:5GSL"
FT TURN 184..189
FT /evidence="ECO:0007829|PDB:5GSL"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:5GSL"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 244..270
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 324..340
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:5GSL"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 416..428
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 448..455
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 478..484
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:5GSL"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 518..530
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 552..557
FT /evidence="ECO:0007829|PDB:5GSL"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 575..580
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 583..590
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 595..604
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 607..615
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 618..626
FT /evidence="ECO:0007829|PDB:5GSL"
FT HELIX 636..647
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 653..658
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 680..686
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 689..695
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 697..709
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 712..725
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 737..745
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 750..759
FT /evidence="ECO:0007829|PDB:5GSL"
FT STRAND 761..777
FT /evidence="ECO:0007829|PDB:5GSL"
SQ SEQUENCE 778 AA; 91169 MW; A5A5E754017615E1 CRC64;
MVGMKVQHDG RLYSLDDERI VVYGGTLQYF RVPRNYWEDR LRKMKSHGLN TVETYIAWNW
HEPQEGVFDF TGETHPQRDL IGFLELAQKL GLYVIIRPGP YICGEWKNGG IPDWLINSHP
EILAKSPNGS FPRDVYYPPI TYLHPTYLEY AMKWYEEVLP IIRDYLYSNG GSIISVTIDD
EPSYWETIFQ PFLTDYNEII VRENGIWHSW LKENYSLGDL EERYGERFSD YTEIAPPKSF
SEPLPKVLDW HHFKIWMINE YVRRLYEKIR EYVDVPISLL DPYLLLAAWK EFYLYVTRHK
LDIHLWTEFW YSFYRTFDFK EDKLGHLYFK TGIYRYYVSK LKTPPLSIET QASLANVIEK
DEAELLYALL PALGIHNLNY YLYVGGENPR GYESHNGVTW DVYSPIGLDG RERQHVEPIK
WIGEFLKSNI DFVDSQFKAR VAFGMYEPYE ALNLWGYKPE SFEESVNLNE YLFGERGLLT
LLAMSNVPFD VIDLEISTLE EMLQYEQIWV YSLDFMSREV QEKLIKYVEE GGNLVILPTL
PYLDENMKPC TRLRDFLGVE VERAKARDNM RLIPYLSVDA EGIDRMVVRN VAREVKGGEA
IAWIGDKVVG TIVRKGKGSA VILGFRLQYY SSYHDMHRKF VDKILQLQGV KREVEVSNRD
IIAIPRIHYL VLVNPRDEEV AGKVKYRGVE FEIKMKGRGV LFIPVDVEIN GVKLVYATAT
PIGGGNRRIK FRNHLSDTSE IAIRDGRIRG VKGGYVLQEK GERVYVIRHE RETFEIEF
