ID A0A1I2UZ86_9BACT Unreviewed; 359 AA.
AC A0A1I2UZ86;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SFG80151.1};
GN ORFNames=SAMN04487988_108113 {ECO:0000313|EMBL:SFG80151.1};
OS Algoriphagus hitonicola.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=435880 {ECO:0000313|EMBL:SFG80151.1, ECO:0000313|Proteomes:UP000199642};
RN [1] {ECO:0000313|EMBL:SFG80151.1, ECO:0000313|Proteomes:UP000199642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19315 {ECO:0000313|EMBL:SFG80151.1,
RC ECO:0000313|Proteomes:UP000199642};
RA de Groot N.N.;
RL Submitted (OCT-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; FOPC01000008; SFG80151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2UZ86; -.
DR STRING; 435880.SAMN04487988_108113; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000199642; 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:UniProtKB-KW.
DR CDD; cd18619; GH43_CoXyl43_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
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 Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 169
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 359 AA; 40526 MW; 788447AFB5AE255D CRC64;
MKFSIHFLTA LVLATGCSQP QKSSEVENTE TVQSKFAHSP LVEDIYTADP SAHIFEGKIY
IYPSHDIETE VQEDDMGSHF DMKDYHVFSM DQPGGEVTGH GVALKLEDVP WAGRQLWAPD
AAEKDGKYYL YFPAKDKADI FKIGVAISDR PEGPFTAEPE PIAGTFSMDP AVFHEGEDYF
LLFGGIWGGQ LQWYENQELV EGRKGPTDGI PAAEEKALMP YIAKLDRSMT KLAEKPRELL
ILDENGEPIK AGENDKRFFE AAWMHEYEGK YYLSYSTGDT HFIAYATGDN PYGPFTYQGN
VLEPVEGWTN HHSIVEFEGK WYLFYHDTEL SGKTPLRNIK MAELTHLPDG KIQTINPMN
//
