ID I3I5N8_9GAMM Unreviewed; 372 AA.
AC I3I5N8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Beta-xylosidase/alpha-L-arabinfuranosidase, putative, gly43G {ECO:0000313|EMBL:EIK43373.1};
GN ORFNames=O59_003771 {ECO:0000313|EMBL:EIK43373.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK43373.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK43373.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK43373.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) 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:EIK43373.1}.
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DR EMBL; AICM01000009; EIK43373.1; -; Genomic_DNA.
DR RefSeq; WP_007645028.1; NZ_JH668205.1.
DR AlphaFoldDB; I3I5N8; -.
DR STRING; 1134474.O59_003771; -.
DR PATRIC; fig|1134474.3.peg.3593; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_1_6; -.
DR OrthoDB; 9760116at2; -.
DR Proteomes; UP000003395; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 184
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 372 AA; 40804 MW; 5E90041B862563EB CRC64;
MNFSKSLLTL ALGAALLSSG CGDKNAQRGT ATTISSAASS ESAPAIDTTK FIGQPLVSHI
YTADPSAHVF NGRIYIYPSH DIDSGITSDG EGDKFDMKDY HVLSMEKIGG EVTDHGVALT
LEDIPWASRQ LWAPDAAEKE GKFFLYFPAK DKDGIFRIGV ATSDSPSGPF AAEPNPIEGS
FSIDPSVFKD DDGSHYLYFG GIWGGQLQRW VSGSYVEEDK YPASNEPALS PKVARLNDNM
LQLAEAPRDI QILDNAGKPL LGSDTNRRFF EGAWLHKFNG KYYFSYSTGD THYIAYATGD
SPYGPFTHQG IVLMPVLGWT NHHSIVEVDG KWFLFYHDSQ LSGGKTYLRN VKVTELIHND
DGTIRTVDAY LD
//
