ID A0A0H4C9D9_9ACTN Unreviewed; 826 AA.
AC A0A0H4C9D9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=QR97_29585 {ECO:0000313|EMBL:AKN73355.1};
OS Streptomyces sp. PBH53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN73355.1, ECO:0000313|Proteomes:UP000036399};
RN [1] {ECO:0000313|EMBL:AKN73355.1, ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|EMBL:AKN73355.1,
RC ECO:0000313|Proteomes:UP000036399};
RX PubMed=26227608;
RA Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT Urban Environment.";
RL Genome Announc. 3:e00859-e00815(2015).
RN [2] {ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA Gosse J.T., Boddy C.N., Hill P.B.;
RT "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT urban environment.";
RL Submitted (JUN-2015) 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; CP011799; AKN73355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4C9D9; -.
DR STRING; 1577075.QR97_29585; -.
DR PATRIC; fig|1577075.3.peg.6176; -.
DR Proteomes; UP000036399; Chromosome.
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; IPR003305; CenC_carb-bd.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 Pfam; PF02018; CBM_4_9; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
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:UP000036399};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..826
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005205240"
FT DOMAIN 467..817
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
SQ SEQUENCE 826 AA; 89605 MW; B749E2E331663788 CRC64;
MSRTARWRLG LGASAVLLAT AALPAPAHAE DVTDYAITVD PSATGPKIDK TMYGVFFEDI
NRAADGGLYA ELVQNRSFEY STADNASYTP LTAWTVSGTA RVVDDSGRLN DRNRAYLSLA
AGSSVTNAGY NTGVAVRDGE KYDFSVWARA EAGSTLAVTL QDAGGALADA RRIAVKKSGW
TRYKATFTAT RTSTAGRLTV AADAATALDM VSLFPRDTYK HEPNGLRKDL AEKIAALSPG
FVRFPGGCLV NTGSMQDYSE GSGWQRKRSY QWKDTIGPVE TRATNANFWG YNQSYGLGYY
EYFRFAEDIG AMPLPVVPAL VTGCGQNKAV VDDALLKRHI QDTLDLIEFA NGPATSEWGK
KRAEMGHPEP FHLTHIEVGN EENLPHEFFA RFQQFRAAVK AKYPSVQVIS NSGPDDAGAT
FDTAWKLNRD ARVDMVDEHY YNSPQWFLQH NDRYDSYDRS GPKVFLGEYA SQGNAFKNGL
AEAAFMTGLE RNADVVKLAS YAPLFANEDY VQWSPDLVWF NNHASWNSAN YEVQKLFMTN
VGDRVVPSTA TGTPSLSGPL TGAIGLSTWN TGAAYDDVKV TAADGGTLFG DDFSGDASRW
THTGTGSWTV RDGSYVQTDD TAENTMVQAG DPSWHDYDLH VKATKKSGKE GFLVAFGVKD
TGNYYWWNLG GWNNTQSAVE QATDGGKSTL LAKAGSVETG RAYDIDIKVR GRQVTLYLDG
KEWGSFADDK PAEPFRQVVT RDAKTGELIV KVVNAQSAAA RTSVDLGGAR VASTAKVTTL
AAAPEAVNTE TSTAVAPKTS TFTGVAGKFT YTFPANSVTF LRIKQK
//
