ID A0A2A2GEY4_9BACT Unreviewed; 324 AA.
AC A0A2A2GEY4;
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 {ECO:0000313|EMBL:PAU95425.1};
GN ORFNames=CK503_03880 {ECO:0000313|EMBL:PAU95425.1};
OS Aliifodinibius salipaludis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX NCBI_TaxID=2032627 {ECO:0000313|EMBL:PAU95425.1, ECO:0000313|Proteomes:UP000218831};
RN [1] {ECO:0000313|EMBL:PAU95425.1, ECO:0000313|Proteomes:UP000218831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN023 {ECO:0000313|EMBL:PAU95425.1,
RC ECO:0000313|Proteomes:UP000218831};
RA Liu D., Zhang G.;
RT "Aliifodinibius alkalisoli sp. nov., isolated from saline alkaline soil.";
RL Submitted (AUG-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:PAU95425.1}.
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DR EMBL; NSKE01000002; PAU95425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2GEY4; -.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000218831; 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; cd18618; GH43_Xsa43E-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:UP000218831};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 169
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 324 AA; 36364 MW; 30E86204C5BBBC96 CRC64;
MGVFVAALLV FSCSTQESTE EVLTDEPVPE PGNPIITEKY TADPAAIVYK DTVFLYVGHD
QAEPGHGFYD LREWLVYSST DLVNWQEYDV PLCAKDFEWA SGDAWAAEVI HHDGKFYWYT
TVTHAENEAK AIGVGVSDSP TGPFKDARGS ALVTNDMTTD VDITWDDIDP TVFVDSDGQA
YMFWGNTQLY YSKLKENMIE LEGEIKTIDL PHFTEGPWIH KKNGYYYLSY AYKFPEKTAY
AMSDNIEGPY YFKGILNEVA GNTNTNHQAI IDYKGQSYFF YHTGAIPTEG GSYRRSVSVD
SLHYNADGTL QKVQMTTEGV GAVE
//
