ID K2Q6L2_9FLAO Unreviewed; 454 AA.
AC K2Q6L2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:EKF56516.1};
GN ORFNames=I215_03298 {ECO:0000313|EMBL:EKF56516.1};
OS Galbibacter marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF56516.1, ECO:0000313|Proteomes:UP000007364};
RN [1] {ECO:0000313|EMBL:EKF56516.1, ECO:0000313|Proteomes:UP000007364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX PubMed=23209227; DOI=10.1128/JB.01852-12;
RA Lai Q., Li C., Shao Z.;
RT "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL J. Bacteriol. 194:6973-6973(2012).
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:EKF56516.1}.
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DR EMBL; AMSG01000002; EKF56516.1; -; Genomic_DNA.
DR RefSeq; WP_008990535.1; NZ_AMSG01000002.1.
DR AlphaFoldDB; K2Q6L2; -.
DR STRING; 555500.I215_03298; -.
DR PATRIC; fig|555500.3.peg.683; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000007364; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PF03422; CBM_6; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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:UP000007364};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT DOMAIN 323..454
FT /note="Cellulose binding type IV"
FT /evidence="ECO:0000259|SMART:SM00606"
FT SITE 165
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 454 AA; 51442 MW; F2C272F5BABFBBCB CRC64;
MNTAFLNFKI HTILKLLFFL VLSVSYGQNP LITDQFTADP TARVFNGKLY VYPSHDIIPP
EGQGRAEWFN MADYHVFSSE NLTEWEDHGV ILSQKDVPWG DPEAYSMWAP DIMERDGKYY
FYFPNRIKDA DDGEGGFSIG VAISDTPEGP FKAHPTPIEG VEGIDPNVFI DKDGQGYLFW
SQSKIYGAKL KDNMLELASE PKTFMELPQK GHMEGPFVFE RDGLYYMTYP HVANKTERLE
YAVSDHPLGT YTHKGVIMDE SAKGTWTNHH SITKYKDQWY LFYHDSELSP NFDKTRSIRA
DSLFFDNNGN IKKVLPTLRG VGISSAYNEI QFDRYSSVNG SGVRFEYLDA QDTFKGWMLV
FTDPDATVRY NKVDFGDTSP KELLVNVNVT HKSTGSLEIR DASGNVIAQT SLNPTDGFKA
VTIPIDPKLT GVKDLLLELK GKGVIQIDWL QFVK
//
