ID A0A1T4N4H3_9FIRM Unreviewed; 459 AA.
AC A0A1T4N4H3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SJZ74132.1};
GN ORFNames=SAMN02745110_01472 {ECO:0000313|EMBL:SJZ74132.1};
OS Eubacterium ruminantium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=42322 {ECO:0000313|EMBL:SJZ74132.1, ECO:0000313|Proteomes:UP000189857};
RN [1] {ECO:0000313|EMBL:SJZ74132.1, ECO:0000313|Proteomes:UP000189857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17233 {ECO:0000313|EMBL:SJZ74132.1,
RC ECO:0000313|Proteomes:UP000189857};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FUXA01000008; SJZ74132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4N4H3; -.
DR OrthoDB; 1771685at2; -.
DR Proteomes; UP000189857; 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; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd18620; GH43_XylA-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000189857};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 140
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 459 AA; 51389 MW; B619565F1D9E5C14 CRC64;
MANPYLPKWE YIPDGEPRVF GDRIYIYGSH DKAGNGEFCD CVLKCWSAPV TNPNEWVCHG
DIFRVGKTRD YDSDTDYTTD NSKLFAPDVI EKDGKYYLYA YIEGQNGCVA VSDRPEGPFK
FLSQTKCNTP GAFNDGIFID PAVFVDDDGR AYIYCGYLKS ELAELNADNM YEVIDGTIIK
DFIPSEVDAE AGFDTNEKLF FEAASMRKIG DTYYMIYSPN DCPKLAYATS DSPTGPFKFR
GFIIDSGADY PGGNDHGSIM NVNGQWYVFY HRMTNGTIMS RRGCVEKIEI LPDGSIPMVE
TTCLGFENAL NPYQITDADL ACVLTGGAFI SERNVFSRFI RNITDETIIG YRYFDFGEDF
GSKTMEFAAK VRGLGGDCRM NIYIDGVDSA DKLTTVKTVG KKIGSITIGH DDEVITEVVE
AVTGVHAVYF TIETDYSGWM ADYFKGRPLF ELESFVFMK
//
