ID I0BJV5_9BACL Unreviewed; 328 AA.
AC I0BJV5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:AFH62652.1};
GN ORFNames=B2K_18320 {ECO:0000313|EMBL:AFH62652.1};
OS Paenibacillus mucilaginosus K02.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH62652.1, ECO:0000313|Proteomes:UP000007392};
RN [1] {ECO:0000313|EMBL:AFH62652.1, ECO:0000313|Proteomes:UP000007392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K02 {ECO:0000313|EMBL:AFH62652.1,
RC ECO:0000313|Proteomes:UP000007392};
RA Xiao B., Sun L., Xiao L., Lian B.;
RT "Complete genome sequence of Paenibacillus mucilaginosus K02.";
RL Submitted (JUN-2013) 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; CP003422; AFH62652.1; -; Genomic_DNA.
DR AlphaFoldDB; I0BJV5; -.
DR KEGG; pmw:B2K_18320; -.
DR PATRIC; fig|997761.3.peg.3614; -.
DR HOGENOM; CLU_009397_4_1_9; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000007392; Chromosome.
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 140
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 328 AA; 36999 MW; B62DC26DBDF26C4F CRC64;
MLSKPVKPGE PLVTHIYTAD PSAHVFDGKI YIYPSHDLDR NHASNDNGDQ YDMEDYHVLS
MEDTESACID HGEALHVKNV PWASKQMWAP DAAYKNDTYY LFFPARDQED IFRIGVAKGA
SPAGPFLPEP QYIPGSFSID PAVFVDEDNR AYMYFGGLWG GQLEKWQTGK FIADAEGPGP
DEPALGPRVA ELSEDMLTFR EAPEEIIILD EQGNPLTAGD EDRRYFEGPW VHKYRGLYYL
SYSTGTTHKI VYAVSADPKG PFVFKGTILT PVIGWTTHHS IVQFQGKWYL FYHDSSLSGG
ADNKRCVKFT ELEYLEDGTI RTIDPYDK
//
