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   24-JAN-2024, entry version 88.
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; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; 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 /
RC   NBRC 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}.
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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; 31958.SD37_25235; -.
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   CDD; cd04082; CBM35_pectate_lyase-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR043534; EBDG/EBM.
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; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43536:SF1; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 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; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
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
//