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Database: UniProt
Entry: U4THP3_9LACO
LinkDB: U4THP3_9LACO
Original site: U4THP3_9LACO 
ID   U4THP3_9LACO            Unreviewed;       783 AA.
AC   U4THP3;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE            EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN   ORFNames=L248_2454 {ECO:0000313|EMBL:ERL63684.1};
OS   Schleiferilactobacillus shenzhenensis LY-73.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Schleiferilactobacillus.
OX   NCBI_TaxID=1231336 {ECO:0000313|EMBL:ERL63684.1, ECO:0000313|Proteomes:UP000030647};
RN   [1] {ECO:0000313|Proteomes:UP000030647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LY-73 {ECO:0000313|Proteomes:UP000030647};
RX   PubMed=24265500;
RA   Lin Z., Liu Z., Yang R., Zou Y., Wan D., Chen J., Guo M., Zhao J., Fang C.,
RA   Yang R., Liu F.;
RT   "Whole-Genome Sequencing of Lactobacillus shenzhenensis Strain LY-73T.";
RL   Genome Announc. 1:e00972-e00913(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC         residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC         Evidence={ECO:0000256|ARBA:ARBA00001462};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC       {ECO:0000256|ARBA:ARBA00007186}.
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DR   EMBL; KI271621; ERL63684.1; -; Genomic_DNA.
DR   RefSeq; WP_022531035.1; NZ_KI271621.1.
DR   AlphaFoldDB; U4THP3; -.
DR   STRING; 1231336.L248_2454; -.
DR   eggNOG; COG3534; Bacteria.
DR   HOGENOM; CLU_010060_2_0_9; -.
DR   OrthoDB; 9758333at2; -.
DR   Proteomes; UP000030647; Unassembled WGS sequence.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31776; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR   PANTHER; PTHR31776:SF0; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          441..771
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
FT   REGION          738..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  86384 MW;  D3D6235E27523AF2 CRC64;
     MTEKVPTITV HPDQPLADLG DLYGIFFEDL NHAADGGLYA EMVQNRSFEF CSVDAPDYHA
     LTAWEDAQGA PLTPAPLALR VLSDAPLNSN NLHYLQIDTH DPRTFRNHGY GQGMAFRRDA
     VYRFSVFARK LYAPVTLTVA LTDDAGQILA SGETVVTSDD WHQYFLTLTS RGTTAAGRLQ
     LTVSGNAHVS LDMISLFPKD TFHHRINGVR EDIGEQLAAL HPRFMRFPGG CLVHDGSLDP
     RDRDAGYRWK NTIGPVEARP ARRNSWGYNQ TLGLGYYELF QLAEDIGAKP LPVLPGGWDP
     HHQWAAPMAE LQPFIDDALD LIEFANGPVD SEWGAKRAAM GHPQPFHLEY LAIGNEEVGQ
     EFFDRYPRFH NQIKARYPDI KLINSAGPFA AGSEFDRGWT SARQHHSDLV DEHYYMSPRW
     FLANQHRYDT YDAHGPKVFL GEYASHGNTW ANALAEASYM IGLERNAAKV GLACYAPLLC
     NTDYVNWRPD LIWYDQQHVT GSVNYDVQKL FMTHQGSQNI AHEEANLPAP LPLPAAPTTG
     AVRFQGADAD ITYSNISYTD LLSDTTTQLA DGTVTGQDQV PLLAKTSGYF RLTFDFVKTG
     GRPDKGMRLD FGVVDDQHRF GWSLGGWQNQ DALIEQIDEG GGSALTQSIW HVSQNVPYHC
     ELTVDGDHLT GKIDGHVFND VRIPSGTIPA LYINSVRTTA GQTIVKLVNV QDTANDARIA
     GLPEGAATIE TLQAPPAAEN TVGQPDQVQQ DNATGQPAAD GTLPVHVPAH SIVFVMTEGS
     KKE
//
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