DEXT_ARTSD
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 25-MAY-2022, entry version 80.
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; Actinobacteria; Micrococcales; 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}.
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; D00834; BAA00708.1; -; Genomic_DNA.
DR AlphaFoldDB; P39652; -.
DR SMR; P39652; -.
DR CAZy; GH49; Glycoside Hydrolase Family 49.
DR PRIDE; P39652; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033904; F:dextranase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 1.
DR Gene3D; 2.60.350.10; -; 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; SSF101596; 1.
DR SUPFAM; SSF51126; SSF51126; 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
