ID V4P7T5_9CAUL Unreviewed; 315 AA.
AC V4P7T5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:ESQ81325.1};
GN ORFNames=AEYBE204_03005 {ECO:0000313|EMBL:ESQ81325.1};
OS Asticcacaulis sp. YBE204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ81325.1, ECO:0000313|Proteomes:UP000017808};
RN [1] {ECO:0000313|EMBL:ESQ81325.1, ECO:0000313|Proteomes:UP000017808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YBE204 {ECO:0000313|EMBL:ESQ81325.1,
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:ESQ81325.1}.
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DR EMBL; AWGF01000001; ESQ81325.1; -; Genomic_DNA.
DR AlphaFoldDB; V4P7T5; -.
DR STRING; 1282363.AEYBE204_03005; -.
DR PATRIC; fig|1282363.3.peg.596; -.
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:UniProtKB-KW.
DR CDD; cd08990; GH43_AXH_like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF6; -; 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: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:UP000017808};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..315
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004726847"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 156
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 315 AA; 34688 MW; 36C356F918561A8A CRC64;
MTPMRSVLFS TGLLLAAVWA SGAGAGEPIS PRFNADPSPH YFKGKFYLYA TDDASNSGKY
WDSTAWRLYT SKDLKTWKDD GAFLDVKVFK WAKPDAKAWA PEAATRNGKY YFYAPIGGDT
IGVAVADKPE GPYRDARTDA LIDKARDANA GAEPIDPAVL IDDDGQAYLF FGTRVPKVVK
LNTDMVSTSG PIMDVVVTGY PSDDPKKKYG EAPFLHKRNG LYYFSFSTGW PGQIVYGTST
SPVGPFDYRG VILDYLTIST NHQAIIEHKG KSWLFYHDNL LPGGGSHRRS IAIEPLDYNA
DGSIRQVVLK KTTQP
//
