ID V4NAG9_9CAUL Unreviewed; 417 AA.
AC V4NAG9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glycoside hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AEYBE204_10920 {ECO:0000313|EMBL:ESQ78927.1};
OS Asticcacaulis sp. YBE204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ78927.1, ECO:0000313|Proteomes:UP000017808};
RN [1] {ECO:0000313|EMBL:ESQ78927.1, ECO:0000313|Proteomes:UP000017808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YBE204 {ECO:0000313|EMBL:ESQ78927.1,
RC ECO:0000313|Proteomes:UP000017808};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ78927.1}.
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DR EMBL; AWGF01000009; ESQ78927.1; -; Genomic_DNA.
DR AlphaFoldDB; V4NAG9; -.
DR STRING; 1282363.AEYBE204_10920; -.
DR PATRIC; fig|1282363.3.peg.2126; -.
DR Proteomes; UP000017808; 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; cd08986; GH43-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 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 Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000017808};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..417
FT /note="Glycoside hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004722991"
FT SITE 253
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 417 AA; 45908 MW; 8DF93DB01A8F7D58 CRC64;
MNIHRRSILS GGAAAAFWAA GSVAFAQSNS GILYPTYPRP GTPKLDNADN SRRIIPAPAK
DYWPYSGISG AGQPVTKATQ TGGWVSGLID VRYKGPVARK YPVADWGTAD SGSAVAKGLL
PAIRPIWDVH IRDTIVQGGG DGWYYMSGST GDNCWAFTDG IELYRSRDLK KWEYRGLIWS
IERDGTWEKN WTARAGVPFR SIWAPEFHYI NGNYYLCHCI SGVGMGVLKS TTGKPEGPYV
HVISQEPIKG GIDSTLFRDD DGKVYLSWGA GQRIREIKPD FSDFAGDWQD IVYDDSGVDP
AAQKDGKPVR RAGFEGVTIF KRGKTYYLGA CNHHEGRYSF MFVTSDKLTG PYGNRHEGPR
GGGGGNVFRD TSGKWWQTFF GNDDQMPFRE KPGLIAIEFD ASGRVVASAD QPFKPLV
//
