ID A0A2U2PKI7_9SPHI Unreviewed; 1192 AA.
AC A0A2U2PKI7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:PWG81838.1};
GN ORFNames=DDR33_05630 {ECO:0000313|EMBL:PWG81838.1};
OS Pararcticibacter amylolyticus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pararcticibacter.
OX NCBI_TaxID=2173175 {ECO:0000313|EMBL:PWG81838.1, ECO:0000313|Proteomes:UP000245647};
RN [1] {ECO:0000313|EMBL:PWG81838.1, ECO:0000313|Proteomes:UP000245647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJ4-8 {ECO:0000313|EMBL:PWG81838.1,
RC ECO:0000313|Proteomes:UP000245647};
RA Cai Y.;
RT "Pedobacter chongqingensis sp. nov., isolated from a rottenly hemp rope.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:PWG81838.1}.
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DR EMBL; QEAS01000003; PWG81838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2PKI7; -.
DR Proteomes; UP000245647; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18608; GH43_F5-8_typeC-like; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006558; LamG-like.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PWG81838.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000245647};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1192
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015638332"
FT DOMAIN 326..462
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 151
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 1192 AA; 131739 MW; BC6400B71E89B3AE CRC64;
MNKMSAWGCG VAGLLLFVSG AFAQIKHDTP GAGNPIIPGY FADPTVKKFG DTWYIYATTD
GNGGGLGPPQ VWESKDFLNW RMKPMNWPNT PHYWAPDVTR GADGKYYLYY CQPVEIYGAS
GPSPSGPWTP LMPGSEPIVK NYRIPDVITL DGQTFRDDDG KMYMFWGTWG IYPNSGCGIG
LLNSDMKSFS KFSKLPNTVA KDFFEAPFMF KRNGIYYLTY SSGRCEDETY RVQYVMSKTG
PMGPFEYGKN NPVLVTNEDG SVHGPGHQSV ISEGDDFYLV YHRHNNPHSG GGFHRQLCAD
ELEFDSEGNI LKVSPTHEGI GLLAKRTSQT TNLASGKPVQ ASSFYSEDFR PSFATDDNNG
TLWKAADNMH EAWLQIDLEK VVPVKRVQIQ FEYATWYYQY LIEYSTDGKD WRIFADKSAN
RQWGSPMEDY ADVKARFLRI KITGTQYPGL NKAIWNVKVY NDKNREAGQL SDVQPENVPD
QPAGLLIDLD ASLLQAGSTV TEWRNSGASG GKFLASGAKA PYVSLISGKT AVVFSGREYL
ESNFGVPSTC SGNSSFTVSM WVFNPAVEKQ EPVFSWADGR RELSRAVIGY GSDRNEGGVI
HGGWPDQPYK SIPEAGKWHH IAVVFDGTKE RVFVDGKLHS EENKMLFLKR GTHFYLGSSE
WLDYFYKGAL AELKMYDKAL SEDEIKVLSV NGKMSSEVAF LDPTRLSYGR KDSITNEGNA
AGFFICRDAV IEDKGGRISL GTGMSAGFRP SGFLEDKLKS LHAFTVSASV YSESDVSLSA
VTTMFDDLMG NKRKSAYKGT IRKGMWHQVM LVKDQGLEPL VYIDGRLAEK AGEISGEKVK
LRRLNISNLA VFGRAIPLSA IDSSFTEWQR SFEEGLAGLK PVFMQRPHAV SDDMVSMAAD
PSSVKGGKPQ YYFIVKDGIK SMGSGWQEDP SFISYNLRPG NRYLFSFKVK DQYGNISALS
DPVEVKMNTA YFSIYEDSFD GGRDFLAGGM SGSFWDGLTG KLKGSSASKI ASVNGSLILA
SSGSNWDGSE PAGPFLYKET DSDFVIRVEI TDITGLAEKR PVGANEAGLM VRLANGDVPA
GRAERLIQNG IMPGWGIGNL VTNLGDFGRL QTNNASAWEY DRHLQIRKQG DMFYIQSSKD
GHVWYDLPGS PVKRPDLNGP KLQVGIFHAA YGKQAGFGTF DNLRIITPKA KD
//
