ID A0A074KUG7_9BACT Unreviewed; 352 AA.
AC A0A074KUG7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Arabinan endo-1,5-alpha-L-arabinosidase {ECO:0000313|EMBL:KEO71925.1};
GN ORFNames=EL17_20630 {ECO:0000313|EMBL:KEO71925.1};
OS Anditalea andensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO71925.1, ECO:0000313|Proteomes:UP000027821};
RN [1] {ECO:0000313|EMBL:KEO71925.1, ECO:0000313|Proteomes:UP000027821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY1 {ECO:0000313|EMBL:KEO71925.1,
RC ECO:0000313|Proteomes:UP000027821};
RA Yang L., Wei S., Tay Q.X.M.;
RT "Characterization and application of a salt tolerant electro-active
RT bacterium.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KEO71925.1}.
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DR EMBL; JMIH01000034; KEO71925.1; -; Genomic_DNA.
DR RefSeq; WP_035078932.1; NZ_JMIH01000034.1.
DR AlphaFoldDB; A0A074KUG7; -.
DR STRING; 1048983.EL17_20630; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000027821; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18616; GH43_ABN-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
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 SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000027821};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..352
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001695417"
FT ACT_SITE 50
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 167
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:PIRSR606710-2"
SQ SEQUENCE 352 AA; 38897 MW; A8B9905C56682FC1 CRC64;
MKSLINIYCL FVPILLAASC QESNEGNPDV DLPEQENTYI NPVFSPVLAD PTVVKSNGYF
YAYGTEDNWG NEGGHKLVPI IRSKNLVNWE FVRNAFQVKP NWKNAGGIWA PDVTQVGEEY
YMYYSYSTWG DPDAGIGLAI ASGPEGPFID QGKLFLSSEI GVENSIDPFY IEDDGKKFLF
WGSFHGIYAI ELSADGKSVE GEKVHIGHTH LEAAYVYKKD GAYFFFGSEG SCCEGANSTY
QVRVGKSNNL LGPYLDKGGN SIADGNHGEI ILRSNSVNYG FAGPGHNAEI MVDDEGTEWL
LYHAIPKNNP RLDNGTNRRP LMLDKLIWRD GYPTIQGQEP SVTSQKAPAF ND
//
