ID A0A127VC31_9SPHI Unreviewed; 326 AA.
AC A0A127VC31;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Arabinan endo-1,5-alpha-L-arabinosidase A {ECO:0000313|EMBL:AMP98854.1};
DE Flags: Precursor;
GN ORFNames=AY601_1947 {ECO:0000313|EMBL:AMP98854.1};
OS Pedobacter cryoconitis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMP98854.1, ECO:0000313|Proteomes:UP000071561};
RN [1] {ECO:0000313|EMBL:AMP98854.1, ECO:0000313|Proteomes:UP000071561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMP98854.1,
RC ECO:0000313|Proteomes:UP000071561};
RA Lee J., Kim O.-S.;
RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP014504; AMP98854.1; -; Genomic_DNA.
DR RefSeq; WP_068399847.1; NZ_CP014504.1.
DR AlphaFoldDB; A0A127VC31; -.
DR KEGG; pcm:AY601_1947; -.
DR PATRIC; fig|188932.3.peg.2038; -.
DR OrthoDB; 9803461at2; -.
DR Proteomes; UP000071561; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18827; GH43_XlnD-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000071561};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..326
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007280381"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 156
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 326 AA; 37155 MW; 437B8FFB79767E36 CRC64;
MKRILILFAC SAFGTCLFAQ KKPVKTSGNP IFQGWYADPE AIVFDNKFWV YPTYSAKYEE
QVFMDAFSSS DLVTWKKHDH VLDTADFKWA KKAVWAPSIT KKDNKYYLFF GANDIQSDQE
TGGIGIGVSD RPEGPFKDYL GKPLIDKFYN GAQPIDQFIF KDKDGQYYLI YGGWGHCNIG
KMKPDFTGFV PFEDGKLFKE ITPKGYVEGP YMFIRNGKYY FMWSEGGWTG PDYSVAYAIA
DSPMGPFKRV DKILKQDPKV ATGAGHHSII KHPQTGDYYI VYHRRPLNET NGNHRVTCID
KMEFDADGLI KPVQITFEGV KSNPIK
//
