ID G4H8K3_9BACL Unreviewed; 324 AA.
AC G4H8K3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:EHB68188.1};
DE EC=3.2.1.55 {ECO:0000313|EMBL:EHB68188.1};
GN ORFNames=PaelaDRAFT_0314 {ECO:0000313|EMBL:EHB68188.1};
OS Paenibacillus lactis 154.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB68188.1, ECO:0000313|Proteomes:UP000003891};
RN [1] {ECO:0000313|EMBL:EHB68188.1, ECO:0000313|Proteomes:UP000003891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154 {ECO:0000313|EMBL:EHB68188.1,
RC ECO:0000313|Proteomes:UP000003891};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA Allgaier M., Woyke T.J.;
RT "The draft genome of Paenibacillus lactis 154.";
RL Submitted (SEP-2011) 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; AGIP01000001; EHB68188.1; -; Genomic_DNA.
DR AlphaFoldDB; G4H8K3; -.
DR STRING; 743719.PaelaDRAFT_0314; -.
DR PATRIC; fig|743719.3.peg.331; -.
DR eggNOG; COG3940; Bacteria.
DR Proteomes; UP000003891; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR InterPro; IPR016828; Alpha-L-arabinofuranosidase.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF025414; Alpha-L-arabinofuranosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:EHB68188.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:EHB68188.1}.
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 135
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 324 AA; 36540 MW; 9B9A84A2A0CB832E CRC64;
MRREMEKLPQ TATFHNPIVE QAADPWVWKH TDGFYYFMHT ARDRIELTKS DSLSRIAEGL
KKTIWAPEPG GRYSHNLWAP EIHHVQGKWY VYYTANDGGG DDTRRICVLE NGEDDPMEGE
WTWRGALDTP VPGLDGTVMT LQGQLYFLYA GYGRFPDYGS AIYIMRMLDP WTLTGEHVLL
TAPTLEWEKQ GGMAINEGPV ILHRNGRIFL VYSASTTWSE DYALGMLTMD ASSDPMNPDA
WTKSPEPVFR KSVENGIYAT GHNSFTKSPD GTEDWIVYHA LPEPGADTRL RATRIQKFGW
HPDGTPDFGI PAGDSDALYV PSGE
//