ID W1S2B9_9SPHN Unreviewed; 425 AA.
AC W1S2B9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:ETI63566.1};
GN ORFNames=C100_12075 {ECO:0000313|EMBL:ETI63566.1};
OS Sphingobium sp. C100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI63566.1, ECO:0000313|Proteomes:UP000018867};
RN [1] {ECO:0000313|EMBL:ETI63566.1, ECO:0000313|Proteomes:UP000018867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C100 {ECO:0000313|EMBL:ETI63566.1,
RC ECO:0000313|Proteomes:UP000018867};
RX PubMed=24482512;
RA Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic
RT Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT Arctic Ocean.";
RL Genome Announc. 2:0-0(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:ETI63566.1}.
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DR EMBL; AYOY01000146; ETI63566.1; -; Genomic_DNA.
DR AlphaFoldDB; W1S2B9; -.
DR STRING; 1207055.C100_12075; -.
DR PATRIC; fig|1207055.3.peg.2279; -.
DR eggNOG; COG3507; Bacteria.
DR Proteomes; UP000018867; 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; 1.
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:UP000018867};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 226
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 425 AA; 47527 MW; C1F382B8BBBD64F3 CRC64;
MFALPGWQPA LFSQIYCSDL RMAQYESGLL RWNDDSAIHN DTTKERMIVG KRPMIWGTLP
LALAALTAGC QQQQPAANEA QPAGDAKRAA SDYLSQPLVK DIYTADPSAH VWDGKIYVYP
SHDIDGPTPE DDLGAHFEMR DYRVLRLDKI GGPVTLGPVA LDVKDVPWAE KQMWAPDAAR
KDGTYYLYFP AKDKEGAFRI GVATSKDPMG PFKAQPNPIK GSYSIDPAVF TDDDGQSYMY
FGGIWGGQLQ RNVTGTYDPN GSKTDLEQDD KPALLPRVAK MTGDMLEFAE TPKPVQILDE
QGKPLLGGDH DRRFFEASWM HKYEGKYYFS YSTGDTHYLA YGIGDSPYGP FTYKGRILEP
VEGWTTHHSI VEWNGKWWLF YADTQLSGQT RLRNVKVTEL HYNPDGTIQT INPFLTKASG
GSAQH
//
