ID A0A095C4Y3_9SPHN Unreviewed; 314 AA.
AC A0A095C4Y3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glycosyl hydrolases 43 family protein {ECO:0000313|EMBL:KGB58376.1};
GN ORFNames=FG95_00981 {ECO:0000313|EMBL:KGB58376.1};
OS Sphingopyxis sp. LC363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB58376.1, ECO:0000313|Proteomes:UP000029625};
RN [1] {ECO:0000313|EMBL:KGB58376.1, ECO:0000313|Proteomes:UP000029625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC363 {ECO:0000313|EMBL:KGB58376.1,
RC ECO:0000313|Proteomes:UP000029625};
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 (MAY-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:KGB58376.1}.
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DR EMBL; JNFC01000010; KGB58376.1; -; Genomic_DNA.
DR RefSeq; WP_052182101.1; NZ_JNFC01000010.1.
DR AlphaFoldDB; A0A095C4Y3; -.
DR STRING; 1120705.FG95_00981; -.
DR PATRIC; fig|1120705.3.peg.986; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9760116at2; -.
DR Proteomes; UP000029625; 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 InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006311; TAT_signal.
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; PS51318; TAT; 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:UP000029625};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..314
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001907493"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 154
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 314 AA; 34281 MW; D4B8C2639D78E2E6 CRC64;
MIRRPVLRRA LLAALLAGSA AAVAADAPAP LSFDGADPDF EAADGRYYIY PTNSGGTGRL
HVWTSPDRRH WKKGAELIAL DRIGWIGDDG APRHALWAPD MIAANGRHYL YYSVGPQNPT
PSRIGVATCA GLEGPCTDSG KPLITGGKGF EAIDPAVFVD PASKTPYLYA GGSAGAKLRV
WTLKPDMVTI DREIAVETPP HFTEGAFMHE RGGTYYLSYS SGSYRHDSYQ VHYATAPSPT
GPWTWRGKIV ESDDRFKGPG HHAFLHDPAD GRWYIAYHRW EGQTGPGPYK GSRKFIVQPI
AYRADGTIVP LEMR
//
