EBDG_AMYOR
ID EBDG_AMYOR Reviewed; 1032 AA.
AC Q56F26;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Exo-beta-D-glucosaminidase {ECO:0000312|EMBL:AAX62629.2};
DE Short=GlcNase {ECO:0000303|PubMed:16316314};
DE EC=3.2.1.165;
DE AltName: Full=Exochitinase {ECO:0000303|PubMed:16316314};
DE Flags: Precursor;
GN Name=csxA {ECO:0000312|EMBL:AAX62629.2};
OS Amycolatopsis orientalis (Nocardia orientalis).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=31958;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAX62629.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 47-60 AND 610-619,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 19795 / DSM 40040 / CBS 547.68 / JCM 4235 / KCTC 9412 / NBRC
RC 12806 / NCIMB 12945 / M43-05865;
RX PubMed=16316314; DOI=10.1042/bj20051436;
RA Cote N., Fleury A., Dumont-Blanchette E., Fukamizo T., Mitsutomi M.,
RA Brzezinski R.;
RT "Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define
RT a new subfamily within family 2 of glycoside hydrolases.";
RL Biochem. J. 394:675-686(2006).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2351651; DOI=10.1016/s0021-9258(19)38783-6;
RA Nanjo F., Katsumi R., Sakai K.;
RT "Purification and characterization of an exo-beta-D-glucosaminidase, a
RT novel type of enzyme, from Nocardia orientalis.";
RL J. Biol. Chem. 265:10088-10094(1990).
RN [3] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-1032 IN COMPLEX WITH
RP BETA-1,4-D-GLUCOSAMINE TETRASACCHARIDE, AND ACTIVE SITES.
RX PubMed=18976664; DOI=10.1016/j.jmb.2008.10.031;
RA van Bueren A.L., Ghinet M.G., Gregg K., Fleury A., Brzezinski R.,
RA Boraston A.B.;
RT "The structural basis of substrate recognition in an exo-beta-D-
RT glucosaminidase involved in chitosan hydrolysis.";
RL J. Mol. Biol. 385:131-139(2009).
CC -!- FUNCTION: Hydrolyzes chitosan and chitooligosaccharides with retention
CC of anomeric configuration. Has maximum activity on chitotetraose,
CC chitopentaose and their corresponding alcohols, with a slight decrease
CC in the rate of hydrolysis on longer chains. Has no activity against
CC beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-
CC D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-
CC D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.
CC {ECO:0000269|PubMed:16316314, ECO:0000269|PubMed:2351651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of chitosan or chitosan oligosaccharides to remove
CC successive D-glucosamine residues from the non-reducing termini.;
CC EC=3.2.1.165; Evidence={ECO:0000269|PubMed:16316314,
CC ECO:0000269|PubMed:2351651};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5 with chitotriitol as substrate, and 5.3 with
CC (GlcN)2 as substrate. Activity is lost below pH 3.5 and above pH 8.0.
CC {ECO:0000269|PubMed:16316314, ECO:0000269|PubMed:2351651};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Stable below 50 degrees
CC Celsius, inactive above 60 degrees Celsius.
CC {ECO:0000269|PubMed:16316314, ECO:0000269|PubMed:2351651};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16316314,
CC ECO:0000269|PubMed:18976664, ECO:0000269|PubMed:2351651}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16316314,
CC ECO:0000269|PubMed:2351651}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY962188; AAX62629.2; -; Genomic_DNA.
DR PDB; 2VZO; X-ray; 2.24 A; A/B=2-1032.
DR PDB; 2VZP; X-ray; 1.05 A; A/B=906-1032.
DR PDB; 2VZQ; X-ray; 1.70 A; A/B=906-1032.
DR PDB; 2VZR; X-ray; 1.95 A; A/B=906-1032.
DR PDB; 2VZS; X-ray; 1.85 A; A/B=2-1032.
DR PDB; 2VZT; X-ray; 2.20 A; A/B=2-1032.
DR PDB; 2VZU; X-ray; 2.10 A; A/B=2-1032.
DR PDB; 2VZV; X-ray; 2.70 A; A/B=2-1032.
DR PDB; 2X05; X-ray; 2.30 A; A/B=2-1032.
DR PDB; 2X09; X-ray; 2.40 A; A/B=2-1032.
DR PDBsum; 2VZO; -.
DR PDBsum; 2VZP; -.
DR PDBsum; 2VZQ; -.
DR PDBsum; 2VZR; -.
DR PDBsum; 2VZS; -.
DR PDBsum; 2VZT; -.
DR PDBsum; 2VZU; -.
DR PDBsum; 2VZV; -.
DR PDBsum; 2X05; -.
DR PDBsum; 2X09; -.
DR AlphaFoldDB; Q56F26; -.
DR SMR; Q56F26; -.
DR STRING; 1125971.ASJB01000069_gene367; -.
DR CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; ag:AAX62629; -.
DR eggNOG; COG3250; Bacteria.
DR BRENDA; 3.2.1.165; 315.
DR EvolutionaryTrace; Q56F26; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0052761; F:exo-1,4-beta-D-glucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR043534; EBDG/EBM.
DR InterPro; IPR028829; Exo-b-D-glucosamin.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041351; Ig_GlcNase.
DR PANTHER; PTHR43536; PTHR43536; 1.
DR PANTHER; PTHR43536:SF1; PTHR43536:SF1; 1.
DR Pfam; PF16990; CBM_35; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF18368; Ig_GlcNase; 1.
DR SUPFAM; SSF49303; SSF49303; 3.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT PROPEP 33..46
FT /evidence="ECO:0000255, ECO:0000269|PubMed:16316314"
FT /id="PRO_0000399046"
FT CHAIN 47..1032
FT /note="Exo-beta-D-glucosaminidase"
FT /evidence="ECO:0000269|PubMed:16316314"
FT /id="PRO_5000095799"
FT DOMAIN 909..1032
FT /note="CBM6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT REGION 883..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 469
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:18976664"
FT ACT_SITE 541
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:18976664"
FT CONFLICT 58
FT /note="V -> VN (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 219..238
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 242..255
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2X09"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 373..385
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 440..455
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 474..486
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 521..525
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 534..542
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 551..557
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 560..568
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:2VZU"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 587..597
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 603..628
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 636..642
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 664..672
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 675..680
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 682..684
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 686..691
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 697..708
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 713..724
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 726..728
FT /evidence="ECO:0007829|PDB:2VZV"
FT STRAND 729..735
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 744..753
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 759..770
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 793..797
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 803..811
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 815..825
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 828..830
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 833..841
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 852..855
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 857..860
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 865..873
FT /evidence="ECO:0007829|PDB:2VZS"
FT HELIX 874..877
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 883..888
FT /evidence="ECO:0007829|PDB:2VZS"
FT TURN 889..891
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 892..897
FT /evidence="ECO:0007829|PDB:2VZS"
FT STRAND 909..912
FT /evidence="ECO:0007829|PDB:2VZP"
FT HELIX 913..915
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 916..924
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 935..938
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 945..965
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 968..970
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 974..978
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 981..987
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 999..1007
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 1009..1018
FT /evidence="ECO:0007829|PDB:2VZP"
FT STRAND 1026..1032
FT /evidence="ECO:0007829|PDB:2VZP"
SQ SEQUENCE 1032 AA; 110633 MW; 150778589094F223 CRC64;
MSFRQKRTRI PLLAMTVTAL AAAVCGVTTA PAATGAEVAV PLSVGAAAGN ATPIPGYVIQ
SSAQVSDDSA VSKPGFPTSG WYPVSSRSTV YAGLLQNGKY ADPFYSTNMQ NVPAAQFSVP
WWYRTDLNVD DTSSRTYLDF SGVLSKADVW VNGTKVATKD QVNGAYTRHD LDITAQVHTG
VNSVAFKVYP NDPNRDLSMG WIDWAQTPPD QNMGIVRDVL VRRSGAVALR SAHVIQKLNS
ALDHADLTVK ADVRNDSANA VQTTVAGTVA GKPISQTVSL AAKERKTVTF PLVGLDRPNV
WWPAGMGGQH RYDLDLTASV GGTPSDAAKS KFGVRDVKAT LNSSGGRQYS VNGKPLLIRG
GGYTPDLFLR WNETAAADKL KYVLNLGLNT VRLEGHIEPD EFFDIADDLG VLTMPGWECC
DKWEGQVNGE EKGEPWVESD YPIAKASMFS EAERLRDHPS VISFHIGSDF APDRRIEQGY
LDAMKAADFL LPVIPAASAR PSPITGASGM KMNGPYDYVP PVYWYDKSQK DRGGAWSFNS
ETSAGVDIPT MDTLKRMMSA SELDTMWKNP SAKQYHRSSS DTFGNLKLFG DALTKRYGAS
ANLNDFVRKA QLSQYENVRA EFESHSRNYT DSTNPSTGLI YWMLNSPWTS LHWQLFDAYM
DQNGAYYGAK KANEPLHIQY SHDNRSVVVI NQTSNAVSGL TATTKLYNLD GTEKYSNTKT
GLSVGALGAK ATAVTVPAVS GLSTTYLAKW VLTDSSGKEV SRNVYWLSTK ADTLNWGGSD
WYYTPQSAFA DLSGLNNLGQ SAVGATANSV AGADGTTTTT VTLKNTSGGR LPAFYVDSKV
VDSAGKPVLP VEWNDNAVSL WPGETTTLTA KYRTADLKGS KPSVRISGWN TGTQTVPADG
SGPGPSDPVD YQAEDATIVQ GAVESNHAGY TGTGFVNYDN VAGSSVEWTV TVPSAGTYDV
VVRYANGTTT SRPLDFSVNG SISASGVAFG STGTWPAWTT KTVRVTLAAG VNKIKAVATT
ANGGPNVDKI TL
