ASL1_BACSE
ID ASL1_BACSE Reviewed; 11 AA.
AC P83146;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 11-DEC-2019, entry version 25.
DE RecName: Full=Acharan sulfate lyase 1;
DE EC=4.2.2.-;
DE Flags: Fragment;
OS Bacteroides stercoris.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=46506 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=HJ-15;
RX PubMed=11322884; DOI=10.1046/j.1432-1327.2001.02156.x;
RA Kim B.-T., Hong S.-W., Kim W.-S., Kim Y.S., Kim D.-H.;
RT "Purification and characterization of acharan sulfate lyases, two novel
RT heparinases, from Bacteroides stercoris HJ-15.";
RL Eur. J. Biochem. 268:2635-2641(2001).
CC -!- FUNCTION: Degrades acharan sulfate and, to a lesser extent, heparin and
CC heparan sulfate. {ECO:0000269|PubMed:11322884}.
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+) ion, nitrogen and cobalt.
CC Activated by reducing agents, such as DL-dithiothreitol and 2-
CC mercaptoethanol. {ECO:0000269|PubMed:11322884}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2.;
CC Temperature dependence:
CC Optimum temperature 45 degrees Celsius.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11322884}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:11322884}.
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DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heparin-binding; Lyase.
FT CHAIN <1..>11
FT /note="Acharan sulfate lyase 1"
FT /id="PRO_0000064700"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:11322884"
FT NON_TER 11
FT /evidence="ECO:0000303|PubMed:11322884"
SQ SEQUENCE 11 AA; 1395 MW; 01B2DAA241E865AB CRC64;
NYIYSGHNYH Q