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Database: UniProt
Entry: Q026H9_SOLUE
LinkDB: Q026H9_SOLUE
Original site: Q026H9_SOLUE 
ID   Q026H9_SOLUE            Unreviewed;       660 AA.
AC   Q026H9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE            EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
DE   Flags: Precursor;
GN   OrderedLocusNames=Acid_2100 {ECO:0000313|EMBL:ABJ83090.1};
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC   Solibacter.
OX   NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ83090.1};
RN   [1] {ECO:0000313|EMBL:ABJ83090.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ83090.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Janssen P.H., Kuske C.R., Richardson P.;
RT   "Complete sequence of Solibacter usitatus Ellin6076.";
RL   Submitted (OCT-2006) 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}.
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DR   EMBL; CP000473; ABJ83090.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q026H9; -.
DR   STRING; 234267.Acid_2100; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   KEGG; sus:Acid_2100; -.
DR   eggNOG; COG3534; Bacteria.
DR   HOGENOM; CLU_413708_0_0_0; -.
DR   InParanoid; Q026H9; -.
DR   OrthoDB; 9758333at2; -.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
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   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:ABJ83090.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABJ83090.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..660
FT                   /note="non-reducing end alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004163093"
FT   DOMAIN          455..651
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   660 AA;  73082 MW;  5992FF17D2697EA1 CRC64;
     MNRRHFLMSS IAASSAVAPS FAVSSSPGSS DADAAGVTRA AVLLVDTDRV TTAIDRRIYG
     HFLEHINHSV VDGLFAEQIR GCGFEGEDFK TYWEPFSENG SAECVDVEFR NGKKSVRLQV
     EGGRAGIRQG RLFMDAGHTY DGSLWVKHEA GSPQLTLRVI SSKGDPIASA PLAVTGSGWQ
     EVHYSFSSAV RETQASVEIA AAGRGTLLLD FVSMMRADVR RDGMLRPDLL QAVRDLAPPF
     IRWPGGSFAS TYKWKDGIGR HVARRYHPNT FWGGYSDYYG FGTEEFLGLC RKLNSEPLIV
     LAAPGTGSEQ VQYAMDWVHY LNDPPTTEMG RLRAANGHPE PYGVRYFQID NEPMNNGFTP
     EKYAEIVNVY GSRLRAIAPQ ARIVACGQKR SNDMVWSQKV IDLAGKNFDV LGVHNYEYEP
     GSFETGLRRI RDSLSKLRDY VRASAHPRIE IGVLEWNLSR TYDWRAGLHA AGSLMLYEEL
     SPSLTMSCPA LLMRNTTDDP TWTSFIYHDH VSWFPGCAYP VEKLFREHYA ERRLASTSGA
     FRDVPDRRHF FDEISTMRPD DWMPGTVDAI ATGSADGRRI VIKAVNYGAE RTALLMRLQG
     ATVPGKAVAT LHTISAGLTD SASLDRPNAI APVSRAVAYA KDLTVDLDPY TVAVLEIRAE
//
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