HYSA_THECX
ID HYSA_THECX Reviewed; 778 AA.
AC A0A3D9VCI6;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Hyaluronate lyase {ECO:0000303|PubMed:33561520};
DE EC=4.2.2.1 {ECO:0000269|PubMed:33561520};
DE AltName: Full=Hyaluronidase {ECO:0000303|PubMed:33561520};
DE Short=HYase {ECO:0000305};
DE AltName: Full=TcHly8B {ECO:0000303|PubMed:33561520};
DE Flags: Precursor;
GN Name=tchly8B {ECO:0000303|PubMed:33561520};
GN ORFNames=DFJ64_1276 {ECO:0000312|EMBL:REF35884.1};
OS Thermasporomyces composti.
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Thermasporomyces.
OX NCBI_TaxID=696763;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22891 / JCM 16421 / I3;
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=DSM 22891 / JCM 16421 / I3;
RX PubMed=33561520; DOI=10.1016/j.pep.2021.105840;
RA Wang X., Zhang S., Wu H., Li Y., Yu W., Han F.;
RT "Expression and characterization of a thermotolerant and pH-stable
RT hyaluronate lyase from Thermasporomyces composti DSM22891.";
RL Protein Expr. Purif. 182:105840-105840(2021).
CC -!- FUNCTION: Degrades hyaluronic acid into unsaturated disaccharides as
CC the end products (PubMed:33561520). Exhibits very low activity against
CC various types of chondroitin sulfate variants (PubMed:33561520).
CC {ECO:0000269|PubMed:33561520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[hyaluronan](n) = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-
CC acetyl-D-glucosamine + H2O; Xref=Rhea:RHEA:50240, Rhea:RHEA-
CC COMP:12583, ChEBI:CHEBI:15377, ChEBI:CHEBI:132151,
CC ChEBI:CHEBI:132153; EC=4.2.2.1;
CC Evidence={ECO:0000269|PubMed:33561520};
CC -!- ACTIVITY REGULATION: Is salt-dependent and is active over a wide range
CC of NaCl concentrations. Activity is slightly promoted by Ni(2+), and
CC inhibited by most of the tested metal ions, including Li(+), K(+),
CC Ba(2+), Mg(2+), Zn(2+), Ca(2+), Mn(2+) and Al(3+).
CC {ECO:0000269|PubMed:33561520}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.6. Activity is completely abolished above pH 8.6.
CC {ECO:0000269|PubMed:33561520};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Is very stable at
CC temperatures from 0 to 60 degrees Celsius.
CC {ECO:0000269|PubMed:33561520};
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC -!- BIOTECHNOLOGY: Due to its high optimal temperature and stability under
CC a broad pH range and high temperature, TcHly8B could serve as a
CC promising tool for the industrial production of hyaluronate
CC oligosaccharides and promote the further exploitation of hyaluronate
CC lyases with novel properties. {ECO:0000269|PubMed:33561520}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000305}.
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DR EMBL; QTUC01000001; REF35884.1; -; Genomic_DNA.
DR SMR; A0A3D9VCI6; -.
DR EnsemblBacteria; REF35884; REF35884; DFJ64_1276.
DR Proteomes; UP000256485; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.100; -; 1.
DR Gene3D; 2.60.220.10; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR038970; Lyase_8.
DR InterPro; IPR011071; Lyase_8-like_C.
DR InterPro; IPR012970; Lyase_8_alpha_N.
DR InterPro; IPR004103; Lyase_8_C.
DR InterPro; IPR003159; Lyase_8_central_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR38481; PTHR38481; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF02884; Lyase_8_C; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
DR SUPFAM; SSF49863; SSF49863; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome; Signal.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 34..778
FT /note="Hyaluronate lyase"
FT /id="PRO_5017671870"
FT ACT_SITE 200
FT /evidence="ECO:0000250|UniProtKB:Q54873"
FT ACT_SITE 250
FT /evidence="ECO:0000250|UniProtKB:Q54873"
FT ACT_SITE 259
FT /evidence="ECO:0000250|UniProtKB:Q54873"
SQ SEQUENCE 778 AA; 85315 MW; D1CD87B1A13AB08E CRC64;
MSWNRRSFLG ALGVTCLAGA GMVPIVRPRT AAAADEFDLL RERWCSLVTG SGYDPDVEPF
KSRLAALGAE AEQYLTTLAP GETSLWPDLP LDTSTWNMTL SARRLRTMAV AYLVPGTGHT
GNSAMAEAAV TAFDELTTRF YAPPHWWGNW WDWLIGTPQA LNDFCALLYE QLGPELIDRY
VQRVDHYVDP GAIDRTTGAN RGWLCEVTAV RGVLGKSPEM MAKARDGLSP IMVYVTDGDG
FYRDGSFIQH EYYAYTGSYG ISLLQSVSGL FALLAGSTWE IVDPNRQVLF DSIENSFAPF
VYNGLLMDAV AGRVISREAE HDHWRGHLLA ASVLRMAEAG SPEEAKRWRG IVKGWLLRES
EPRYMGDQTL TMAAVADAQA VLDDPTIEPL PEPVEHRIFA AMDQAVHRRP TWAFSISMRS
VRTAFYETIN GENLKGWHTG VGMTYWWGAD FGNDHYTDGF WPTADPYRLP GTTVSRKPLE
DGVGNNVLPT EAWAGGTTDG EFAAVGQSIQ ALESTLRGRK SWFCLDDAVV CLGAGITCAD
GYAVDTTVDQ RNLGENGVHD FRLNGIPSPT SGTWSLTVPN ARWAHLEGFG GYVFPGGARV
SAIRETRTGS WYDINVGGPR DELRRRYVTV YLDHGVDPVD ASYVYLVMPG ATRQETIRRA
ADRRWLRVLA NTADRQAISV PSLGFVGANF FAPGTVDALT VDQPCSVLVR VADGRATICV
SDPRQDGSTV RVTWNRPVAS VVSSDPTVRV VEAGERLVLD VTVEETAGMT QRAVVALA
