ID A0A0J0US85_9ACTN Unreviewed; 402 AA.
AC A0A0J0US85;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glycosyl hydrolase family 43 {ECO:0000313|EMBL:KLR59776.1};
DE Flags: Precursor;
GN ORFNames=IMCC26207_11015 {ECO:0000313|EMBL:KLR59776.1};
OS Actinobacteria bacterium IMCC26207.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1641811 {ECO:0000313|EMBL:KLR59776.1, ECO:0000313|Proteomes:UP000036180};
RN [1] {ECO:0000313|EMBL:KLR59776.1, ECO:0000313|Proteomes:UP000036180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26207 {ECO:0000313|EMBL:KLR59776.1,
RC ECO:0000313|Proteomes:UP000036180};
RA Kim S., Cho J.-C.;
RT "Genome sequence of freshwater Actinobacteria.";
RL Submitted (MAY-2015) 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 -!- 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:KLR59776.1}.
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DR EMBL; LCZK01000010; KLR59776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J0US85; -.
DR STRING; 1641811.IMCC26207_11015; -.
DR Proteomes; UP000036180; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd08999; GH43_ABN-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 Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000036180};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..402
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005244735"
FT TRANSMEM 372..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 24..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 190
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 402 AA; 42970 MW; 70D236E5C4DD1C2A CRC64;
MLVKVLLLIG LSLFAGLISA PPAGAKDPND AQPGQRLPTR GPVKSSSVPK AERDVNLVDG
LLRGVPIVEG DFADPFALAE PDALYIYATN TVDANIPVIR IRKNQLFKAQ YLGDALPTLP
SWTVKGFQWA PSVWAAPGDS FVMYYTTPSS GGLGNKQCIS RATSTDPAGP FVDNSTEAFI
CPLSEGGAID ASIFVDTDDV LYLIWKSDGN CCNLPTVIYS QPLTSDGLSV AGPPVELITA
SQPWEDNLVE GPSMIRKGAT YYLFYSANQW DTTDYAIGAA TCTSVSGPCT KPEEKPWMDS
GTFSKGPGGQ EFFESAGKPG VWMVHHGWLP NQAGTPGGQR RLYLDKLGFQ QGDTLPTRTG
KAAAAEALVQ DALIVGLVLA AIIGLWFLVR SLLRRRKQKS AA
//
