ID A0A0P7C3X5_9BACT Unreviewed; 345 AA.
AC A0A0P7C3X5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:KPM47851.1};
GN ORFNames=AFM12_11445 {ECO:0000313|EMBL:KPM47851.1};
OS Jiulongibacter sediminis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Jiulongibacter.
OX NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM47851.1, ECO:0000313|Proteomes:UP000050454};
RN [1] {ECO:0000313|EMBL:KPM47851.1, ECO:0000313|Proteomes:UP000050454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN14-9 {ECO:0000313|EMBL:KPM47851.1,
RC ECO:0000313|Proteomes:UP000050454};
RA Liu Y., Du J., Shao Z.;
RT "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL Submitted (JUL-2015) 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:KPM47851.1}.
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DR EMBL; LGTQ01000009; KPM47851.1; -; Genomic_DNA.
DR RefSeq; WP_055148299.1; NZ_LGTQ01000009.1.
DR AlphaFoldDB; A0A0P7C3X5; -.
DR STRING; 1605367.AFM12_11445; -.
DR PATRIC; fig|1605367.3.peg.3687; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000050454; 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; cd18619; GH43_CoXyl43_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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000050454};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 151
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 345 AA; 38667 MW; D691EB7A360A1341 CRC64;
MPEDSIEHID FKELNEKAIS QPLVTNIYTA DPSAHVFEGK IYIYPSHDID AGDAFDDLGS
HFAMEDYHVI SMDSVDSPVV DHGVALHVDD VPWAEKQMWA PDAHEKDGKY YLFFPAKAYD
GIFRIGVAIG DSPVGPFKAQ PEAIKGSFSI DPAVYKDDDG EYYMYFGGIW GGQLQRWRTG
EFNAGQPESP FAFIPEDDEP ALCAKIAKLT PDLLEFAEEP KDVVILDENG EALLAGDTDR
RFFEAAWVYK HNGKYYFTYS TGDSHFICYA TGDSPYGPFT YGGRILEPVV GWTTHHSVCQ
VEGKWYLFYH DSSLSKGVTH LRSIKVAEII HNEDGSIQTL KPYGD
//
