ID A0A1W6LG64_9BURK Unreviewed; 312 AA.
AC A0A1W6LG64;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Name=abnA {ECO:0000313|EMBL:GLS97190.1};
GN ORFNames=A4W93_26705 {ECO:0000313|EMBL:ARN23206.1}, GCM10007918_44820
GN {ECO:0000313|EMBL:GLS97190.1};
OS Piscinibacter gummiphilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=946333 {ECO:0000313|EMBL:ARN23206.1, ECO:0000313|Proteomes:UP000193427};
RN [1] {ECO:0000313|EMBL:ARN23206.1, ECO:0000313|Proteomes:UP000193427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS21 {ECO:0000313|EMBL:ARN23206.1,
RC ECO:0000313|Proteomes:UP000193427};
RA Tabata M., Kasai D., Fukuda M.;
RT "Complete genome sequence of natural rubber-degrading, novel Gram-negative
RT bacterium, Rhizobacter gummiphilus strain NS21.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GLS97190.1, ECO:0000313|Proteomes:UP001157201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109400 {ECO:0000313|EMBL:GLS97190.1,
RC ECO:0000313|Proteomes:UP001157201};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GLS97190.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 109400 {ECO:0000313|EMBL:GLS97190.1};
RA Sun Q., Mori K.;
RT "Draft genome sequence of Rhizobacter gummiphilus strain NBRC 109400.";
RL Submitted (JAN-2023) 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}.
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DR EMBL; CP015118; ARN23206.1; -; Genomic_DNA.
DR EMBL; BSPR01000017; GLS97190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6LG64; -.
DR STRING; 946333.A4W93_26705; -.
DR KEGG; rgu:A4W93_26705; -.
DR OrthoDB; 9801455at2; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000193427; Chromosome.
DR Proteomes; UP001157201; 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; cd18829; GH43_BsArb43A-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000193427};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..312
FT /note="Extracellular exo-alpha-(1->5)-L-
FT arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030037086"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 152..155
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 172..174
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT SITE 155
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 312 AA; 33749 MW; A3CADD8FC1967CAD CRC64;
MFTKRFRRQA LAAAALASAI LPASAAHWAL TGDVGAHDPS ILREGDRWFT FSTGEGLQVL
AGDSTGRNWT RAPRIFLSPP SWWKTYVPNQ KANDVWAPDA HQFNGKVWVY YAISSFGSNT
SAIGLVSATK VSDGRWTDNG LVLRSTSAND YNAIDPNLVI DASGNPWLAF GSFWSGLKIV
RLNPSTMKPT GSQTSIAKRS AGIEAPAITY NNGWYYLFAS IDKCCQGVNS TYKIIYGRSR
SITGPYLDKA GKSLLSGGGT VFDAGNARWK GPGGQDVGHG VIARHAYDAT DNGNPKLLIS
DLKWTSDGWP TY
//
