ID W4CR43_9BACL Unreviewed; 296 AA.
AC W4CR43;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glycoside hydrolase family protein {ECO:0000313|EMBL:ETT58570.1};
GN ORFNames=C173_30677 {ECO:0000313|EMBL:ETT58570.1};
OS Paenibacillus sp. FSL R7-277.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT58570.1, ECO:0000313|Proteomes:UP000019051};
RN [1] {ECO:0000313|EMBL:ETT58570.1, ECO:0000313|Proteomes:UP000019051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT58570.1,
RC ECO:0000313|Proteomes:UP000019051};
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 glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:ETT58570.1}.
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DR EMBL; ASPX01000118; ETT58570.1; -; Genomic_DNA.
DR AlphaFoldDB; W4CR43; -.
DR PATRIC; fig|1227352.4.peg.6149; -.
DR eggNOG; COG3507; Bacteria.
DR Proteomes; UP000019051; 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; cd18827; GH43_XlnD-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 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:ARBA00022651};
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 Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 134
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 296 AA; 33491 MW; FE54A20A71BF531F CRC64;
MRGITNPVIP GWYADPEART YGGRHYVYAT RSFTEYTRQM NLDAFSSGDL VHWTTHEGII
EMDDFPWIWR AVWAPTQIEH HGRHYLVFAS NDIQKDGEAG GLEIAVADAP EGPYRGYLHR
PLIGGFVHGA QPIDAHLFKD DDGAIYLYYG GWGHCNVARM NEEMTGFVPF PDGEVILSVT
PPGYVEGPCM IKKDGLYYLM WSMGGWTNGT YRVAYGVSDN PLGPFPNLGT ILERQEPVAE
GPGHHGYLHL PDRDEWLIVY HRRLIGDREP GNRMLCIDRL ELGAGVIKPV RMTDRW
//
