ID   DEXT_ARTSD              Reviewed;         640 AA.
AC   P39652;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   05-FEB-2025, entry version 87.
DE   RecName: Full=Dextranase;
DE            EC=3.2.1.11;
DE   AltName: Full=Alpha-1,6-glucan-6-glucanohydrolase;
DE   AltName: Full=Endodextranase;
DE   Flags: Precursor;
OS   Arthrobacter sp. (strain CB-8).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=74565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 50-61.
RX   PubMed=1859672; DOI=10.1266/jjg.66.173;
RA   Okushima M., Sugino D., Kouno Y., Nakano S., Miyahara J., Toda H., Kubo S.,
RA   Matsushiro A.;
RT   "Molecular cloning and nucleotide sequencing of the Arthrobacter dextranase
RT   gene and its expression in Escherichia coli and Streptococcus sanguis.";
RL   Jpn. J. Genet. 66:173-187(1991).
CC   -!- FUNCTION: Efficiently decomposes water-insoluble glucan as well as
CC       dextran.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in
CC         dextran.; EC=3.2.1.11;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0.;
CC       Temperature dependence:
CC         Optimum temperature is 42 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 49 family. {ECO:0000305}.
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DR   EMBL; D00834; BAA00708.1; -; Genomic_DNA.
DR   AlphaFoldDB; P39652; -.
DR   SMR; P39652; -.
DR   CAZy; GH49; Glycoside Hydrolase Family 49.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033904; F:dextranase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.350.10; Dextranase, N-terminal; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR041402; B_solenoid_dext.
DR   InterPro; IPR035953; Dextranase_N-ter.
DR   InterPro; IPR005192; Glyco_hydro_49_C.
DR   InterPro; IPR023226; Glyco_hydro_49_N_dom.
DR   InterPro; IPR041274; IPU_b_solenoid.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF18841; B_solenoid_dext; 1.
DR   Pfam; PF03718; Glyco_hydro_49; 1.
DR   Pfam; PF17433; Glyco_hydro_49N; 1.
DR   Pfam; PF18783; IPU_b_solenoid; 1.
DR   SUPFAM; SSF101596; Dextranase, N-terminal domain; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   PROPEP          33..49
FT                   /evidence="ECO:0000269|PubMed:1859672"
FT                   /id="PRO_0000012211"
FT   CHAIN           50..640
FT                   /note="Dextranase"
FT                   /id="PRO_0000012212"
FT   REGION          248..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   640 AA;  71289 MW;  E9D9833A203602B6 CRC64;
     MPGTGLGRLA KRMTAAAAVF FISTSAVLPA QAATAPAAAP PGVPAALKAE RAITTVDNGN
     LHTWWHDNGV FSPATPTQSS EVRRSSFYDV QVAQANQPQK LYDAFSYMSI PRSGKGKIGY
     TEEDGAEFSS DARLTMSWSS FEYAKDVWVE VSLRTGQTIS SADQVQIRPS SYNFEKQLVD
     ADTVRIKVPY SDAGYRFSVE FEPQLYTAYN DMSGDSGKLT TEAAGNRPIH TEPRNSMMVF
     AEPKLRGEQK ERLVPTEESG SIHYPEPGEV RNLNSVSEEI IYFRPGTYSM GPDYHAVLPA
     NVKWVYLAPG AYVKGAFRFL HDTQSQYKVT GYGVLSGEQY VYEADTNNSY HHLSGASNCH
     SSCVKMLQFA SADAEQKLDL QGVTVAEPPY HSFVVYGNEQ TFHMNVENYK QVGSWYWQTD
     GIELYKGSTM KNTFFNANDD VLKMYHSDVT IDNTVIWKNE NGPVIQWGWT PRNIDNVNVA
     NTTVIHNRMY WKDVKYNTCI FNSSSHWEDM GSTTKADPNT TVKNMRFENT AVEGMTNCAI
     RVYALSDTEN IHIKNFNIGA WNGLEWTSQV SHLKRYTNSA GEKVTIGNEV PDGNGLALEN
     YSVGGQVIEK TGGNSSDYQL GRLGFDGENW ENWNAWKSAP
//