ID A0A2C1YW02_9BACI Unreviewed; 511 AA.
AC A0A2C1YW02;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Glycoside hydrolase 43 family protein {ECO:0000313|EMBL:PGV49306.1};
GN ORFNames=COD92_22580 {ECO:0000313|EMBL:PGV49306.1};
OS Bacillus sp. AFS037270.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV49306.1, ECO:0000313|Proteomes:UP000225442};
RN [1] {ECO:0000313|EMBL:PGV49306.1, ECO:0000313|Proteomes:UP000225442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS037270 {ECO:0000313|EMBL:PGV49306.1,
RC ECO:0000313|Proteomes:UP000225442};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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:PGV49306.1}.
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DR EMBL; NUNF01000048; PGV49306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1YW02; -.
DR Proteomes; UP000225442; 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; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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}.
FT DOMAIN 314..506
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 124
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 511 AA; 57583 MW; 29B4CD799902B738 CRC64;
MKYTNPVISG FHPDPSVCKV GDDFYLVTSS FEYFPGIPIF HSKDLVNWEQ IGHVLTLESQ
LPLTRQHSHV RSQGIYAPTI RHHNGRFYVI TTNITIMKSF YVWADQPDGP WSEPIFIEGW
RGYDPSLFFD NDGKVYLTGA SFPGFGTEAI FQAEIDLETG ELVSENQMIW EGTGNSSPEG
PHLYKINDWY YLMIAEGGTE FGHMVTIARS RSPYGPFESN PNNPILSNRS SKKQIQATGH
ADLVQATDGT WWAVFLGIRP VKSTKLHHLG RETNLAPVAW SEEGWPVIGN NVRAEVEHDA
KALPLSTTQT WQENDDFDSK SLSHVWNFYR NPDVESWSLT EKPGSLTLNG QPCTLNDTGS
PVFVGRRQQH FNCVVSTLME FSPNQDGEEA GLTVFMNENF HYDIAKTVQY GKSIILYRRR
VGSLWKVERK IEYDEPSVVF TVKATDINFT FSYQSANGVE KVLGSGETSF LSTQIAGGFT
GIYFAMYATG NGKASTTPAH FEYFKYLPEK E
//
