ID A0A0U4B2F6_9BACT Unreviewed; 331 AA.
AC A0A0U4B2F6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=ABC transporter substrate-binding protein {ECO:0000313|EMBL:ALW87245.1};
GN ORFNames=AUC43_05550 {ECO:0000313|EMBL:ALW87245.1};
OS Hymenobacter sedentarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW87245.1, ECO:0000313|Proteomes:UP000059542};
RN [1] {ECO:0000313|EMBL:ALW87245.1, ECO:0000313|Proteomes:UP000059542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5B {ECO:0000313|EMBL:ALW87245.1,
RC ECO:0000313|Proteomes:UP000059542};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|PIRNR:PIRNR026534}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
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DR EMBL; CP013909; ALW87245.1; -; Genomic_DNA.
DR RefSeq; WP_068198266.1; NZ_CP013909.1.
DR AlphaFoldDB; A0A0U4B2F6; -.
DR STRING; 1411621.AUC43_05550; -.
DR KEGG; hyg:AUC43_05550; -.
DR OrthoDB; 9801455at2; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000059542; Chromosome.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:InterPro.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd18830; GH43_CjArb43A-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW Reference proteome {ECO:0000313|Proteomes:UP000059542};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..331
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006847086"
FT ACT_SITE 32
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 149..152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 169..171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT SITE 152
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-3"
FT SITE 285
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-3"
SQ SEQUENCE 331 AA; 35938 MW; 443B2A2279094876 CRC64;
MPKLLLLALL LTCLGATAQT APAATGAIPA HDPVMIRQQG TYYLFCTGNG ITVWSSADRK
TWKPEKPVFA APPAWAVAAV PSFKGHIWAP DISFANGQYS LFYSVSAFGK NTSCIGLATN
KTLDPASPDF KWVDHGRVIQ SVPGRDMWNA IDPNLARDAA GAPWLTFGSF WDGIKLVKLR
PDLTAPAQPE QWRTIAHRSR DPKLNDSLPG DGAIEGPFIF KKGGFYYLFT SFDYCCRGPQ
STYKMMVGRA AGITGPYVDR AGVALDQGGG TVVLAGDSKW YGVGHNAVCS FDNVDYLVFH
GYDASDRGRP KLRIEKLSWD KEGWPAVAAA Q
//
