ID A0A1K1S481_9BACT Unreviewed; 344 AA.
AC A0A1K1S481;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SFW79161.1};
GN ORFNames=SAMN05661012_04730 {ECO:0000313|EMBL:SFW79161.1};
OS Chitinophaga sancti.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1004 {ECO:0000313|EMBL:SFW79161.1, ECO:0000313|Proteomes:UP000183788};
RN [1] {ECO:0000313|EMBL:SFW79161.1, ECO:0000313|Proteomes:UP000183788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 784 {ECO:0000313|EMBL:SFW79161.1,
RC ECO:0000313|Proteomes:UP000183788};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FPIZ01000017; SFW79161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K1S481; -.
DR STRING; 1004.SAMN05661012_04730; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000183788; 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.
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 158
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 344 AA; 38977 MW; D1D6C9BDC0C94CFB CRC64;
MTHLLKICRY AALQGMIYLL ASLQGMTQPL VKHIYTADPS AHVFNNRIYI YPSHDTATGV
PEDDLGSHFD MKDYHILSLD HVGGKVTDHG VALTLKDVPW AQKQLWAPDA AYANNTYYLY
FPAKDSTGVF HIGVAKSSKP EGPFKALPKP IPGSYSIDPC VFKDEDGNFY MYFGGIWGGQ
LQKWDHNKYN SKAGNKAADE KAALPRVAKL KKDMTSFDGQ VKDVVILNEK GLPFYEKDND
KRFFEASWVH KYKGKYYFSY STGDTHNLCY AIGNSPYGPF TYKGVIMTPV KGWTTHHSII
EKDGKWYLFY HDVELSGKTY LRNVKVTELH YKADGSIETI HPEI
//
