EBDG_STRAW
ID EBDG_STRAW Reviewed; 904 AA.
AC Q82NR8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Exo-beta-D-glucosaminidase {ECO:0000312|EMBL:BAC68933.1};
DE EC=3.2.1.165;
DE Flags: Precursor;
GN Name=csxA {ECO:0000312|EMBL:BAC68933.1}; OrderedLocusNames=SAV_1223;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1] {ECO:0000312|EMBL:BAC68933.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Hydrolyzes chitosan and chitooligosaccharides with retention
CC of anomeric configuration. Has no beta-mannosidase activity.
CC {ECO:0000250|UniProtKB:Q56F26, ECO:0000269|PubMed:16316314}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.3. {ECO:0000269|PubMed:16316314};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q56F26}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q56F26}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000255}.
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DR EMBL; BA000030; BAC68933.1; -; Genomic_DNA.
DR RefSeq; WP_010982661.1; NZ_JZJK01000078.1.
DR AlphaFoldDB; Q82NR8; -.
DR SMR; Q82NR8; -.
DR STRING; 227882.SAV_1223; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; BAC68933; BAC68933; SAVERM_1223.
DR KEGG; sma:SAVERM_1223; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_2_4_11; -.
DR OMA; VDWNPYP; -.
DR OrthoDB; 245411at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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; 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; 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; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..904
FT /note="Exo-beta-D-glucosaminidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399047"
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 476
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q56F26"
FT ACT_SITE 545
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q56F26"
SQ SEQUENCE 904 AA; 97183 MW; C68F8507993D4C18 CRC64;
MFHRPASVRR FVTTAVALGL LSTLSTGARA GARTHEPPPR PTTVSSTAGS TTALTGYAIQ
STAKVTDPAA AVSSPGYPAS GWYPAGARST VLAALLAGGK YADPFYSTNQ QKIPKADFQV
PWWYRSDFTV ADTSARTYLD FSGVISAADV FVNGRQIARS ADVAGAYTRH ELDVTSLVRE
GANTVAFRIQ PNNPNKNLTM GWIDWLEPPP DQNMGIVRDV LVRRGGPVAL RDAHVITRLD
VPSLATADLT VKARARNDSD AAITATVSGS VGATSFRRSV ALAAHETKTV TFTPADTPGL
HLTSPRVWWP AGMGGQPLYA LDLSASVSET VSDTVHESFG IRDVKAPLNS DGARQYSVNG
RRLLIKGGGW SPDEFLRWDS TYVEDRLRYA LDLGLNTIRL EGHIEPDEFF DLADRYGILT
LPGWECCNKW EGNVNGSGSG DEWTAADYPV AKASMAAEAA RLRDHPSVVS FLIGSDFAPD
AKIEKTYLDA LKAADWPTPV VAAASDKSSP VSGSSGMKMT GPYDWIPPNY WYAKREGGAT
GFNSETSAGP DIPTLDTLRR MMTPAELDTL WKNPGAKQYH RSPSSVFGTL KIYDAALAGR
YGAPTGLTDY VRKAQLAQYE NVRAQFEAYG RGATDASKPA TGVIYWMFNS GWTSLHWQLL
DRYLDQGGAY FGAKKANEPL HVQYSYDDRS VVVVNNRPAA VSGLTARVTL FNTDGTQKYD
KSATGLSVAG DGAHSTALTL PSSVSGLSTT YLARLVLTDS AGKEVSRNVY WLSTRPDTLD
WAHTDWYYTP TTSYADLKGL GSMARVPVSA TASTTAGTDG ASTTTVTVRN TGSGRTPSLF
TDVHLVDSKG KPVLPVQWSD NEVSLWPGES ATLTVTYRTA DLHGSAPRVR VSGWNTAEQT
VPAA
