ID W4AMJ3_9BACL Unreviewed; 986 AA.
AC W4AMJ3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Hyaluronate lyase {ECO:0000313|EMBL:ETT32529.1};
GN ORFNames=C169_23325 {ECO:0000313|EMBL:ETT32529.1};
OS Paenibacillus sp. FSL R5-808.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227076 {ECO:0000313|EMBL:ETT32529.1, ECO:0000313|Proteomes:UP000019053};
RN [1] {ECO:0000313|EMBL:ETT32529.1, ECO:0000313|Proteomes:UP000019053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-808 {ECO:0000313|EMBL:ETT32529.1,
RC ECO:0000313|Proteomes:UP000019053};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000256|ARBA:ARBA00006699}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETT32529.1}.
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DR EMBL; ASPT01000050; ETT32529.1; -; Genomic_DNA.
DR RefSeq; WP_036643211.1; NZ_ASPT01000050.1.
DR AlphaFoldDB; W4AMJ3; -.
DR PATRIC; fig|1227076.4.peg.4791; -.
DR Proteomes; UP000019053; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR CDD; cd01083; GAG_Lyase; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR38481; HYALURONATE LYASE; 1.
DR PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF02884; Lyase_8_C; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ETT32529.1}.
FT DOMAIN 44..193
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 249..554
FT /note="Polysaccharide lyase 8 N-terminal alpha-helical"
FT /evidence="ECO:0000259|Pfam:PF08124"
FT DOMAIN 597..858
FT /note="Polysaccharide lyase family 8 central"
FT /evidence="ECO:0000259|Pfam:PF02278"
FT DOMAIN 873..936
FT /note="Polysaccharide lyase family 8 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02884"
SQ SEQUENCE 986 AA; 108393 MW; F0DC78FED4A8FE3E CRC64;
MDLGSRRLSM AVVFCMIFQV IFAGLLGSNH QVHASAVEGN QGPNLIPNGG FEEGTLLQHQ
DWVGGRPDGW SAWLPTRNGQ QVSVVNNQSH LGSRSVEIKH QAAARTAVAP QPITPVLPGL
AYTVQAWLKT QDVKPVDAGK GVYIRTQFCA ENGSKLMDGP AIPFVKGSTE WTLHEMKIEV
PKDPRITRLK VEILLETGTG TVWIDDVSLT ETGSDLPAQA FDTIRQRWAS KLVGGEGVQM
NDPDAAANVS ALVERMTNGD KTGRWDTLNK GDHPDSLWDG VISKTQNDSW RISWAYGIIR
DLALAYSIEG SPLYGNEALK NDIVRAMKWM YEYQYNPSKK ITGNWWDWEI GTPQEVMNIL
VLMHDVMPPE LLNQYLAAID KFVPDPKKRV ANPAAVETGA NLLDKALVVT LRGIVGKQAS
KIEMGRDSIT DEFLYVKQGD GVYEDGSLVQ HKNIAYTGSY GGVLLGRMAD LFLLFADSPW
AITDPNARHV YDWVGRSFEP LIYKGAMMDS VKGRSISRAA DSDHLAGRSV SMTILRLAQS
APPAQASQMK SMVKEWALKD TTFDNYYTGL PLYELNLLKQ LMQDDSVMPR GELVHTQVFA
GMDRAVQLRE HFGLGISMFS DRISAFEYGN GENAKGWYTG MGMTSLYNQD LKQFSDQYWP
TVDSYRLPGT TTDRSSKAPA EWGYYMNSRD WVGGSVIDGE YGAVGMEFAL DQSTGSSLSG
KKSWFLFDDE MVALGSDIKN LSGNPTETIV ENRQLTHAGD NKLIINGREL PPSLGWEEKV
SNVSWAHLEG NVTGADIGYV FPSRQEVAGK REVRVGSWSE INKSGPADPI SRNYLSLAIE
HGTAVSSGSY EYVLLPGKTS QQTAAYAASP DIQVLAATGR VHAVKERKHG LTGINFWDAG
SFQQVTTDQP ISYIMKENGD MLTIAVAEPT QKQTRVVVDV DKSGLQVLAQ DPTVTVLQMS
PSIRLAIDTQ GSAGKSHTIT LRLDPT
//
