HYSA_CUTAC
ID HYSA_CUTAC Reviewed; 812 AA.
AC P0CZ00; Q59634; Q6AAT4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Hyaluronate lyase {ECO:0000303|PubMed:9115089};
DE EC=4.2.2.1 {ECO:0000250|UniProtKB:Q54873};
DE AltName: Full=Hyaluronidase {ECO:0000303|PubMed:9115089};
DE Short=HYase;
DE Flags: Precursor;
OS Cutibacterium acnes (Propionibacterium acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=1747;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=49/51;
RX PubMed=9115089; DOI=10.1139/m97-044;
RA Steiner B.M., Romero-Steiner S., Cruce D., George R.;
RT "Cloning and sequencing of the hyaluronate lyase gene from
RT Propionibacterium acnes.";
RL Can. J. Microbiol. 43:315-321(1997).
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:0000250|UniProtKB:Q54873};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:9115089}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|PubMed:9115089}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA51650.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U15927; AAA51650.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; P0CZ00; -.
DR SMR; P0CZ00; -.
DR CAZy; PL8; Polysaccharide Lyase Family 8.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0030340; F:hyaluronate lyase activity; IEA:UniProtKB-EC.
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; IPR003159; Lyase_8_central_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR38481; PTHR38481; 1.
DR Pfam; PF02278; Lyase_8; 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 Direct protein sequencing; Lyase; Secreted; Signal.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT /evidence="ECO:0000269|PubMed:9115089"
FT CHAIN 33..812
FT /note="Hyaluronate lyase"
FT /id="PRO_0000410486"
FT ACT_SITE 222
FT /evidence="ECO:0000250|UniProtKB:Q54873"
FT ACT_SITE 272
FT /evidence="ECO:0000250|UniProtKB:Q54873"
FT ACT_SITE 281
FT /evidence="ECO:0000250|UniProtKB:Q54873"
SQ SEQUENCE 812 AA; 87758 MW; D72FB62E1439CB96 CRC64;
MFGTPSRRTF LTASALSAMA LAASPTVTDA IAAPGPDSWS ALCERWIDII TGRRAARTSD
PRARAIIAKT DRKVAEILTD LVSGSSRQTV LISADLRKEQ SPFITKTARA IESMACGWAT
PGSSYHKDPE ILSACIEGLR DFCRLRYNPS QDEYGNWWDW EDGASRAVAD VMCILHDVLP
PEVMSAAAAG IDHFIPDPWF QQPGSVKPTA NPVQPVVSTG ANRMDLTRAV MCRSIATGDE
KRLRHAVDGL PDAWRVTTEG DGFRADGGFI QHSHIPYTGG YGDVLFSGLA MLFPLVSGMR
FDIDESARKA FHDQVERGFI PVMYNGQILD DVRGRSISRI NESAAMHGIS IARAMLMMAD
ALPTHRAEQW RGIVHGWMAR NTFDHLSEPS TLVDISLFDA AAKAPRPGVV DAELLRVHGP
SRPATADWLI TVSNCSDRIA WYEYGNGENE WAYRTSQGMR YLLLPGDMGQ YEDGYWATVD
YSAPTGTTVD STPLKRAVGA SWAAKTPTNE WSGGLASGSW SAAASHITSQ DSALKARRLW
VGLKDAMVEL TTDVTTDASR AITVVEHRKV ASSSTKLLVD GNRVSSATSF QNPRWAHLDG
VGGYVFATDT DLSADVATRK GTWIDVNPSR KVKGADEVIE RAYASLHGHP PRSSSPWALL
PTASRSHTMA LATRPGVEPF TVLRNDGNRP GRASAGALLT KDPTVVTTLA FWKPATCGGV
AVNRPALVQT RESANQMEVV IVEPTQKRGS LTVTIEGSWK VKTADSHVDV SCENAAGTLH
VDTAGLGGQS VRVTLARQVT QTPSGGGRHD RA