ID A0A417C831_9FIRM Unreviewed; 1874 AA.
AC A0A417C831;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:RHS91943.1};
GN ORFNames=DW911_09390 {ECO:0000313|EMBL:RHS91943.1};
OS Erysipelatoclostridium sp. AM42-17.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=2293102 {ECO:0000313|EMBL:RHS91943.1, ECO:0000313|Proteomes:UP000284957};
RN [1] {ECO:0000313|EMBL:RHS91943.1, ECO:0000313|Proteomes:UP000284957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM42-17 {ECO:0000313|EMBL:RHS91943.1,
RC ECO:0000313|Proteomes:UP000284957};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RHS91943.1}.
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DR EMBL; QUIN01000026; RHS91943.1; -; Genomic_DNA.
DR OrthoDB; 6636047at2; -.
DR Proteomes; UP000284957; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 2.
DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 4.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 5.
DR Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR000421; FA58C.
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; PF00754; F5_F8_type_C; 5.
DR Pfam; PF07554; FIVAR; 4.
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; 5.
DR SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
DR PROSITE; PS50022; FA58C_3; 5.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:RHS91943.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000284957};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1874
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038641733"
FT TRANSMEM 1852..1869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 712..812
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 836..979
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 980..1121
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1127..1245
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1261..1414
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT COILED 1508..1545
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1874 AA; 213417 MW; FCA097628E213A8F CRC64;
MKKILKVMVS LFVVFTMSLS SIQVTFGLTS SQEIETIKGR LKDYFLSLDT IDDGSKVETC
YVSKADSYLK LIQEDGSFDD VNYKANNNAA NGAAWSPYLA LDRLQAIAIA YSKEGNALYQ
KQEVVEKLEK ALQYWKGQNP RSTNWWENQV GVQLRFSRIA LFLEDVVDDD VENIMLDKLL
EKVPVKYGTG QNNLWFDQNY VYYALLTDDS TRLQDMVENY LSYCLVTQKD NKTAEAVQVD
NSFYMHGKQF YSNGYGMSMF RDMSFWIYML RDTSFSLGED VINRMADYMI NGTSWTIRGD
LQELYLGYRE YKYSVGYKNY AAEYIEPLKR MIASDQVHAK QYQDILNNIE NPQASNGKNG
NYYMWRSGYA SHMRNGYGVN IKMDSDEIIG GEWRGSWPNG NQGQLIYWTS SAASTISVDG
DEYTTVYPTY DWAHCPGTTT AARVVQDYSN AGRFTNGTSH TIGVSNGQYG ATAYAMDKKG
TQVNKGYFFF DDEIVALGSG ITSSESTEIH TTLNQAKADD VLVDGTAISK DTTKEVNDAK
WVYNNKIGYI FPDETTVTVS NAYQKDNPSL WAEEKKETTP RTFKAYINHG LKPNNQSYSY
IILPNQTSDQ VSKYATNNPI TIVANNENIQ AVRHETLKQT QINFYKAGTL EYKKGYKITV
DQPCSLIIDE STDERKMTLA TSDSQSSVTT NVQLEYNNTK TNTTFLSPVA PYTGSSLTLK
ENESNLYQAS SSTSSHEIEC AFDNDETTYW QSQTNGEEWL TIFTGKDQYL SKLNITWGDH
YALDYDIYTS QDGINYTFLK NVNQKTKSNK DSIDINGIYP YIKIVMKKSN DANYQIKEIT
WDQKANLTYK KSVEVSSQYS DELKKENAID GNTNTRWGSK RDSDDNWIIV DLQKNCTINA
IDLLWEAACS DEYSIEVSDD KQNWTVVKDK LKTNESLKDQ YIFDEAVSGR YLKIHSTKTR
IVSGKNYGVS LFELVAYGSE EQEDIDYDNI ALNKPVEVSS QYSEELKKEN AVDGDLKKRW
GSKRASDDNW IIIDLEKYSK INKIQIDWEK ACSDDYTIEV SDDKQNWNVV SESKTNSSLR
DIHTYDDFIY GRYVKIHSYK SRCVSNTNYG IGINEVEVYG KESSVVNQNQ NIALNKPAYS
SSTFKSEHST SKAFDGSKES RWVSVRKKEN QNKNVDYQWI YVDLENYYDI SKIVLDWEGA
CATDYKIQIS SNGKNWKDLS VVNDGKSGER TFDYADQSIA RYVRVECLKP SGIYGYSLWE
FEVYGLRVKQ PTTTNLALNK KAYASSEYKS QYGASKAFDG SEDATKDKES RWVSLRQKDN
KKDVSNQWIY VDLDDYYNIN QIKLNWEGSG ATEYKIQVSL DGKDWQDISN ITNGNGGIET
YNYNGVTARY VKMQGVKPGS IYGYSLWEVE VYGEALDKSE LTNLYYMNLD IDTSVYTPSS
SERFKQALDD ALKVMNDADA TSSSILKAKQ DLQDSITGLT KLASFDYLKT LIDEYSKLDE
TLYTSASFEQ LKDKLAKAQD VYNDKNSSQE TVDNMCNELT EAKNQLVLKG DKTDLIALME
EIKKLDRSLY LEATLNELDT YLQKAQTVVD NDQATNDDVL KAYQDLYNVR DNLVTQESYQ
NLKALLDKVE NVDESKYTDQ SLQVLKTKYQ QAKDAYEKAV PKKDEIAKAT QELQQAFNSL
QLKVNKEKLQ NTIIKATSID RSQYTPASLL KLDSEVAKAK ALLDKVDVTQ TEIDDMTKSL
TTMLNSLVLK ADKNKLSQLV KEIEKLDLGQ YQNTGKLITL LNQSKELLNN DNATQAEIDQ
MYSSLQNAYK QIEKVNNDKT GSNDTVQENK TVNENVNKKE NVETKDTDST NLTGLFVILM
MSLLGIIFIK KRIS
//
