ID A0A1Q4X3L5_9ACTN Unreviewed; 840 AA.
AC A0A1Q4X3L5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=A6A08_06915 {ECO:0000313|EMBL:OKI16993.1};
OS Nocardiopsis sp. TSRI0078.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1718951 {ECO:0000313|EMBL:OKI16993.1, ECO:0000313|Proteomes:UP000185866};
RN [1] {ECO:0000313|EMBL:OKI16993.1, ECO:0000313|Proteomes:UP000185866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0078 {ECO:0000313|EMBL:OKI16993.1,
RC ECO:0000313|Proteomes:UP000185866};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI16993.1}.
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DR EMBL; LWLB01000023; OKI16993.1; -; Genomic_DNA.
DR RefSeq; WP_073703295.1; NZ_LWLB01000023.1.
DR AlphaFoldDB; A0A1Q4X3L5; -.
DR STRING; 1718951.A6A08_06915; -.
DR Proteomes; UP000185866; 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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..840
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012750096"
FT DOMAIN 480..830
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
FT REGION 795..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 91508 MW; E957C2BE2BD1080D CRC64;
MRANRRRSAR TACALITGLL CAVTAAAPAS AATDYSITVD PSATGPRISD QMYGIFLEDI
NHAADGGLYA ELVQNRSFEY GTADNENYTP MTAWEEITTG NADGWAKVVN DDGRLNERNR
NYLRLVLPAD GEYGVVNSGY STGITVTEGE EYDFSVWAKS PGHAVPLTVR LHDAQGGPLA
EPLTLDVQGR RWARYTGTLT ATGSSTTGRL SVTGSGGGVL GLDMVSLFPR ETFKGRENGL
RADIAERIAE LAPGFVRFPG GCLVNTGSHE AYEGPDWPRE RSYQWKDTVG PVEERATNHN
FWGYNQSYGL GYYEYFQFAE DLGAMPLPVV PALVTGCGEN EATDDPDLLR RHIQDTLDLI
EFANGPADSE WGSVRAEMGH PEPFGLTHVQ VGNEENLPDA FFENFLRFRD AIEAEYPDIT
VVGNSGPASG GTVFERAWEL NREHGVDMVD EHYYNSPAWF LANNERYDSY DREGPDVYLG
EFASQGNQFS NALAEAAYMT GLERNADVVK MASYAPLLAA EWGTQWTPDM IWFDNSTSWG
SANYEVQRLF STNTGDRVVP STASGTPGIG GPITGAVGLS TWNTSAEYDD VRVTSADGET
LLADDFSSGA DQWTHVTGAG NWTVENGAYV QTEVSGENTM VTAGDPGWTD YDLEVTATKR
EGAEGFLIGF GVQGTGDYYW WNLGGWNNTQ SAVERASDGE KSLIVSDGTT VEAGRAYDIR
VEVRDRDVTL YLDGEEWDSF TAPEPEPFRQ VVTRDEQTGE LIVKVVNAQD EAARTSIDLG
SARVEPTAEL TVLQADPAAE NTATDRPVSP ETSTIDGVGS TFTHTFPAHS VTFMRLAPER
//
