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Database: UniProt
Entry: A0A0H2KWJ9_9MICO
LinkDB: A0A0H2KWJ9_9MICO
Original site: A0A0H2KWJ9_9MICO 
ID   A0A0H2KWJ9_9MICO        Unreviewed;      1267 AA.
AC   A0A0H2KWJ9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=FB00_04345 {ECO:0000313|EMBL:KLN36234.1};
OS   Cellulosimicrobium funkei.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Cellulosimicrobium.
OX   NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN36234.1, ECO:0000313|Proteomes:UP000035265};
RN   [1] {ECO:0000313|EMBL:KLN36234.1, ECO:0000313|Proteomes:UP000035265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U11 {ECO:0000313|EMBL:KLN36234.1,
RC   ECO:0000313|Proteomes:UP000035265};
RA   Hu C., Gong Y., Wan W., Jiang M.;
RT   "Cellulosimicrobium funkei U11 genome.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KLN36234.1}.
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DR   EMBL; JNBQ01000002; KLN36234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2KWJ9; -.
DR   STRING; 264251.FB00_04345; -.
DR   PATRIC; fig|264251.5.peg.896; -.
DR   Proteomes; UP000035265; 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; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041542; GH43_C2.
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   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF17851; GH43_C2; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035265};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1267
FT                   /note="non-reducing end alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005200344"
FT   DOMAIN          803..1158
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   1267 AA;  134516 MW;  832607310B71293E CRC64;
     MTGLVGTVAL ATSLPASAAE PDLPDDARVD AFDGSTLGAD WTVVNPVPEA LAVSGGALRL
     TSQPGDTYQD ANSAKNVVLM DVPAGDFTVV TRLEAPVASV YQGAGLIAWQ DMDNYVRSGL
     TFVGSLSPSG RAIENDVETG GVFSAAAFTD RPASTGETLR MQRTGDTIAT SYWDGAAWQP
     AGSVTVDFPT TQVGLYALAA QNGAAHTAAF DYVALQTAEG ADQVPDGPFT LAGPGDARYL
     VATDDGLALD DERPATTVAL DATAVDGAEG TSPVTLAVDD RPVVVSDASR LSLGAAGDDA
     TALRLTDAGG GKVWLRDSAD PERYAGVRAS DGALVLGPRD SATKLTITPA TSADHEITVD
     LAGERTEMSD ELYGIFYEDI NYAADGGLYA ELVRNRSFEF NHQDNGSFTG LTAWSAANRG
     GATATTQVVN DAGRLNATNR NYLNLTTTAA GAGVRNAGYN TGLFVEEGES YDFSVWARSA
     TAQTVTVRVE DNAGTTAYAT GQVAVDGSNA WKKYDVALTA TGTTNAGRLA LLSGAAGTLA
     LDQVSLFPQD TWVGPVNGPS VLRKDLAEKI DALDPQFLRF PGGCVTNVGT FRTYEESGFT
     DRRRTYQWKE TIGPVEERAT NWNFWGYNQS YGIGYLEYFL FAEDLGATPL PVVSVGANGC
     GSTIPEMKDP AQIQRWVDDT VDLIEFANGD VTTEWGAVRA GLGHPEPFGL KYIGLGNEEN
     TKTFEANFPA FRDAIAAAYP DIQIISNSGP DDTGQRFDEL WEFNREQDVD LVDEHYYNDP
     QWFLENDERY DSYDREGPHV FLGEYASRGN TFANALAEAS FMTGLERNSD VVRLASYAPL
     LANESYVQWS PDAIWFDNDE SWGSVNYYVQ QLFSANAGDE VVPSTHSGPA PADATLDGGV
     FLSTWNTAAQ YDNVRVTDNA SGDVLFADDF ESGASQWEPQ TGTWAAQDGA YVQSATNVTD
     ARSIVAGAYA KDWSSYTLEL DARKTSGAEG FLVGFAAGGP NDYYWWNLGG WNNTRQALQR
     ASGGSANEVK AVENHSIEVG QPYHVKVVVE GSTIELYLDG ELQMSYEQPS TKSLYQVVTR
     DDDTGDVVVK VVNPTATAAR TQVHVEGAEG IASEATVTEM VGAPSDTNTK ADPERVVPVE
     RTLTGVGEEF SYEFPAHSIT FVRLHASDAA PELDLAVEAS PRCLAGKAYV AVRATNGEDV
     PVSVTLSTPF GQKAFAGVAP GKSAYQSFTA RATSAPAAVA TATGTATLDG EQVTSTVDVA
     YDALDCG
//
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