ID A0A085EQF3_9BURK Unreviewed; 319 AA.
AC A0A085EQF3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Arabinoxylan arabinofuranohydrolase XynD {ECO:0000313|EMBL:KFC61448.1};
DE EC=3.2.1.55 {ECO:0000313|EMBL:KFC61448.1};
GN Name=xynD_4 {ECO:0000313|EMBL:KFC61448.1};
GN ORFNames=FG94_05089 {ECO:0000313|EMBL:KFC61448.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC61448.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC61448.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC61448.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) 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:KFC61448.1}.
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DR EMBL; JNNN01000083; KFC61448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085EQF3; -.
DR STRING; 1502852.FG94_05089; -.
DR PATRIC; fig|1502852.3.peg.5005; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9760116at2; -.
DR Proteomes; UP000028601; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
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 Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..319
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001788967"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 160
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 319 AA; 34902 MW; 54DBB025EE98C067 CRC64;
MNKMSVLVAG LAAALAAPLA GASNPIVKDI FTADPAALVD NGRVYLYVGK DEAPVGGKEY
VMSEWRVYSS CDMKKWTDHG SPLRYSTFKW AGRDAWASDI VKRGGKYYFY STVDHAALKS
KAIGVAVSNS PTGPFVDARG TALITNDMTR ETDIPWDDID PAVFIDDDGQ AYLYWGNTVM
KYARLKPNMI ELDGPIHTVG LDNFVEAAYL HKRKGTYYLS YSRKFPEETV VMSGPTATGP
WTFGGVIMEK NSNVNTIHQA IVEFNGKSYI FYHNGKLPTG GEFRRSVAVE ELHYGPDGKM
LPVAQTAEGP AANPSPGCK
//
