ID A0A229TEI3_9PSEU Unreviewed; 522 AA.
AC A0A229TEI3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:OXM69314.1};
GN ORFNames=CF165_07195 {ECO:0000313|EMBL:OXM69314.1};
OS Amycolatopsis vastitatis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM69314.1, ECO:0000313|Proteomes:UP000215199};
RN [1] {ECO:0000313|Proteomes:UP000215199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA Kalinowski J., Ziemert N.;
RT "Comparative genome mining reveals phylogenetic distribution patterns of
RT secondary metabolites in Amycolatopsis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family.
CC {ECO:0000256|ARBA:ARBA00006963}.
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:OXM69314.1}.
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DR EMBL; NMUL01000007; OXM69314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229TEI3; -.
DR OrthoDB; 9804807at2; -.
DR Proteomes; UP000215199; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR GO; GO:0031221; P:arabinan metabolic process; IEA:InterPro.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR InterPro; IPR038964; ABFB.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR39447; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR SUPFAM; SSF110221; AbfB domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..522
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012759713"
FT DOMAIN 46..357
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 375..515
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT ACT_SITE 242
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 321
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 47..57
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 107..112
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 197..198
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 424..462
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 522 AA; 54298 MW; A86AACA5144BEAB1 CRC64;
MSQRRDSKNV SANTRPRILL LLSAAAALVL ASLTTASTAS AATSLPCDIY GAAGTPCVAA
HSTTRALYAA YNGPLYQVQR ASDSARTNIG LLAAGGYANA AAQDSFCAGT TCLITEIYDQ
SPRHNDLTIE GPGGAGGQDT GVPADALPVT AGGHQVYGAS FSGRMGYRDN TTSGVAVNGQ
PEGMYMITSG THVNDRCCFD YGNAETNNLD TGNGHMDALN FGTECWFQPC NGTGPWVQAD
LENGLFQSSA GGSQNTANTG TKFPFVTALL KNNGQNFFAL KDGNAQSGSL RTTYSGPEPT
TGSGYAPMHQ EGAIVLGTGG DNSNGSIGSF FEGVMTAGLP TDAADNAVQA NVVSVGYGGP
TGTTGSLTAG SELSLRATTA CCTGDYLRHQ NDSAVISPVS SGSSTVDKSD ATWIVRKGLA
DASCVSFESR NYPGDFLRHF NFKVQRQPMD GSAAFRADAT FCPVAGKNGQ GTSFRSYNYP
TKYLRHYNFS VYIADTSGTN AWDSATSYND DTSWVAGQPW AP
//
