ID A0A0M2T3C5_9BACI Unreviewed; 327 AA.
AC A0A0M2T3C5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:KKK39772.1};
GN ORFNames=WQ57_00270 {ECO:0000313|EMBL:KKK39772.1};
OS Mesobacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK39772.1, ECO:0000313|Proteomes:UP000034166};
RN [1] {ECO:0000313|EMBL:KKK39772.1, ECO:0000313|Proteomes:UP000034166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA2-6 {ECO:0000313|EMBL:KKK39772.1,
RC ECO:0000313|Proteomes:UP000034166};
RA Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-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:KKK39772.1}.
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DR EMBL; LAYY01000001; KKK39772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2T3C5; -.
DR PATRIC; fig|1408103.3.peg.60; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000034166; 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 Reference proteome {ECO:0000313|Proteomes:UP000034166};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 138
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 327 AA; 36830 MW; 0DF57B1CB281FA71 CRC64;
MKNSKPNEPI VTHIFTADPS AHVFEGKLYI YPSHDLEHDE PSNDNGDQYK MEDYHVLSME
DVDGPCVDHG EVLHLKDIPW ASKQLWAPDA AYKNNTYYLF FPARDKDGIF RIGVATSPSP
AGPFKAEENY IPGSFSIDPA VLVDEDNKAY VYFGGLWGGQ LEKWQTGIYQ HDAAGPAASE
PALGPIAAEL TDDMLNFKSE PKEISIVDEE GNPILAGDED RRYFEGPWVH KYNGLYYLSY
STGTTHKIVY AVSENPMGPF TFKGTILTPV IGWTTHHSIV QYKDKWYLFY HDSSLSGGVN
HKRSVKFTEL KYNEDGTIQT IAPYENK
//
