ID A0A172TQ05_9BACL Unreviewed; 579 AA.
AC A0A172TQ05;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:ANE49062.1};
GN ORFNames=SY83_20030 {ECO:0000313|EMBL:ANE49062.1};
OS Paenibacillus swuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE49062.1, ECO:0000313|Proteomes:UP000076927};
RN [1] {ECO:0000313|EMBL:ANE49062.1, ECO:0000313|Proteomes:UP000076927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6 {ECO:0000313|EMBL:ANE49062.1,
RC ECO:0000313|Proteomes:UP000076927};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL Submitted (JAN-2015) 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; CP011388; ANE49062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A172TQ05; -.
DR STRING; 1178515.SY83_20030; -.
DR KEGG; pswu:SY83_20030; -.
DR PATRIC; fig|1178515.4.peg.4052; -.
DR OrthoDB; 177947at2; -.
DR Proteomes; UP000076927; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076927};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT SITE 169
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 579 AA; 63761 MW; 88C828E4992226CC CRC64;
MTSSVRKIVM ITLGAALLIS IIIWGFSYMN NQETGAAQSE YNGHGGTFKN TLSPMDTPDP
SVVYKDGYYY MTFTHNGTDI MVLKSRTIDF KQAQRKIVWL PDVGTAYSAE LWAPEIQWIQ
GKWYIYFAAD DGLNENHRMF ALQADTEDPM GAYTFKGQIG DASDKWAIDG LVMEYKEKLY
FVWSGWEGDV NERQNTYIAP MSDPLTISGE RVRLSTPDMD WEQAGGPPFI QEGQSILHHE
DRVHIVYSGA GSWTPYYSLG MLSLKENGDP LSAADWVKAE KPLMTMNAKA SVYGPGHNSF
TSSPDGRELW IVYHATSRED DGWNNRKARA AKVTWDENGN PLFGEPLSLR TAIHVPSGTG
LYRPVAQEES PETLVIESVP SSVETNISTL IHYTNNTGKD ALLNVGIQDQ PFAQVSLPSV
ETDGKGFAYV SVKMGNGLND LILDGLPAGV KVEAVEFPRY EAEDAQGKGD AETEENPYAS
GTGIAVLPAD KASSINFSNV CVPVAGTYVL RIAAANSSGG KANVQVSVNG KDYELNLQST
KRNQHLIHEL EVELNSGPNE IILEHAKHSV HMDYMDVSK
//