ID A0A1M7N6K7_9BACT Unreviewed; 336 AA.
AC A0A1M7N6K7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SHM99189.1};
GN ORFNames=SAMN04488057_10594 {ECO:0000313|EMBL:SHM99189.1};
OS Cyclobacterium lianum.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=388280 {ECO:0000313|EMBL:SHM99189.1, ECO:0000313|Proteomes:UP000184513};
RN [1] {ECO:0000313|EMBL:SHM99189.1, ECO:0000313|Proteomes:UP000184513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6102 {ECO:0000313|EMBL:SHM99189.1,
RC ECO:0000313|Proteomes:UP000184513};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FRCY01000005; SHM99189.1; -; Genomic_DNA.
DR RefSeq; WP_073094348.1; NZ_FRCY01000005.1.
DR AlphaFoldDB; A0A1M7N6K7; -.
DR STRING; 388280.SAMN04488057_10594; -.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000184513; 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; cd08981; GH43_Bt1873-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:SHM99189.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184513}.
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 336 AA; 38571 MW; 5807BE361615EE19 CRC64;
MKPLFPLLIF ILLFQYRTFS QNRLPEIREN IPLDSIRLSD PCILADAKTS MYYITGTGGL
LWKSKDLGHW TGPYRVVETD PDSWMGPRPM IWAAELHYYK DKYYNFATFT NREVKIDTVQ
GNVIERRASH ILVSDKAEGP YVPMEDPTYL PADKPTLDGT FWVDEDGKPY MVYCYEWLQN
WNGTIEKIEL KPDLSGSVGK SQLLFKASES PWSRERNDEG DTIPNKVTDG PWLFKTQTGK
LGMIWTSWVF GDYTQGVAYS ESGTLDGPWI HDEQPFSPPN YGHGMLFRTF EGQLLMAVHS
HRVGENGRYI RIPKLFEVDD SGDKLVLGEP FRGNVN
//
