ID A0A0C9MU28_SPHPI Unreviewed; 350 AA.
AC A0A0C9MU28;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Extracellular exo-alpha-(1->5)-L-arabinofuranosidase {ECO:0000256|PIRNR:PIRNR026534};
DE EC=3.2.1.55 {ECO:0000256|PIRNR:PIRNR026534};
GN ORFNames=SP6_31_00180 {ECO:0000313|EMBL:GAN14191.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN14191.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN14191.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN14191.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|PIRNR:PIRNR026534};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|PIRNR:PIRNR026534}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
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:GAN14191.1}.
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DR EMBL; BBJS01000031; GAN14191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MU28; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000032025; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:InterPro.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd08998; GH43_Arb43a-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534}.
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 168..171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 188..190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT SITE 171
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:PIRSR026534-3"
FT SITE 302
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-3"
SQ SEQUENCE 350 AA; 37982 MW; F6390C43142A49B0 CRC64;
MGPLGRCSIM PRAQKPGRAL WLALLLIGAA PAPDKVTPPL SGDIVPTHDP VLIREGDRYY
AYSTGQRGRV PLVARRSPDL IQWTALPSPL AAIPGWALAA VPGARDIWAP DISRVGGRYW
LYYSVSTFGK QRSVIGLATA ATLDPASPHY GWRDEGMVVA SQEGGAFNAI DPAFARDRQG
GQWLAFGSFW DGIQLVRLDP RTGKPASGTK IRTIARRAAG ESEGGGNAIE APFIVDHGGW
YWLIVSFDRC CRGVKSSYHL RVGRARSIEG PYRDREGRAM LDGGGTVLLQ AGATDRYRGP
GHAGVLRDRD GRDYLIHHAY DAEADGASTL RIARLRWDSQ GWPFVEGEAS
//
