ID B9XQQ1_PEDPL Unreviewed; 338 AA.
AC B9XQQ1;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:EEF57833.1};
DE Flags: Precursor;
GN ORFNames=Cflav_PD0815 {ECO:0000313|EMBL:EEF57833.1};
OS Pedosphaera parvula (strain Ellin514).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=320771 {ECO:0000313|EMBL:EEF57833.1, ECO:0000313|Proteomes:UP000003688};
RN [1] {ECO:0000313|EMBL:EEF57833.1, ECO:0000313|Proteomes:UP000003688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin514 {ECO:0000313|EMBL:EEF57833.1,
RC ECO:0000313|Proteomes:UP000003688};
RX PubMed=21460084; DOI=10.1128/JB.00299-11;
RA Kant R., van Passel M.W., Sangwan P., Palva A., Lucas S., Copeland A.,
RA Lapidus A., Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Larimer F.W., Land M.L., Hauser L., Brettin T.S.,
RA Detter J.C., Han S., de Vos W.M., Janssen P.H., Smidt H.;
RT "Genome sequence of 'Pedosphaera parvula' Ellin514, an aerobic
RT Verrucomicrobial isolate from pasture soil.";
RL J. Bacteriol. 193:2900-2901(2011).
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:EEF57833.1}.
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DR EMBL; ABOX02000056; EEF57833.1; -; Genomic_DNA.
DR RefSeq; WP_007418137.1; NZ_ABOX02000056.1.
DR AlphaFoldDB; B9XQQ1; -.
DR STRING; 320771.Cflav_PD0815; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000003688; 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; cd18827; GH43_XlnD-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 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:ARBA00022651};
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:UP000003688};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..338
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002895070"
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 338 AA; 38222 MW; 991A86481B4CC3BA CRC64;
MKRHSFAQPR KLLFTLLVAL SLSALCPLHA ADQTATPEHS GNPIFPGWYA DPEAKIFGKE
FWIYPTYSAK YDEQVFLDAF SSPDLVHWTK HTRVLDTNSV TWARRAMWAP AVAENNGRYF
LFFGANDIQN DHQLGGIGIA VADQPAGPFN DYLGKPLIGQ FHNGAQPIDQ FVFKDQDGQY
YLIYGGWRHC NICRLKNDFR GLEPFADGTT YKEITPEGYV EGSVMFRRGA KYYFMWSEGG
WTGPNYSVAY AMADSPLGPF KRIGKILQQD PKVATGAGHH SVIQLPGKDE WYIVYHRRPL
GETDGNHRVT CIDHMEFDTQ DHIKPVKITF EAVPPAKP
//
