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Database: UniProt
Entry: A0A0Q4KT90_9SPHN
LinkDB: A0A0Q4KT90_9SPHN
Original site: A0A0Q4KT90_9SPHN 
ID   A0A0Q4KT90_9SPHN        Unreviewed;       518 AA.
AC   A0A0Q4KT90;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:KQN27449.1};
GN   ORFNames=ASF00_14230 {ECO:0000313|EMBL:KQN27449.1};
OS   Sphingomonas sp. Leaf34.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN27449.1, ECO:0000313|Proteomes:UP000051932};
RN   [1] {ECO:0000313|EMBL:KQN27449.1, ECO:0000313|Proteomes:UP000051932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf34 {ECO:0000313|EMBL:KQN27449.1,
RC   ECO:0000313|Proteomes:UP000051932};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN27449.1, ECO:0000313|Proteomes:UP000051932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf34 {ECO:0000313|EMBL:KQN27449.1,
RC   ECO:0000313|Proteomes:UP000051932};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers.
CC       {ECO:0000256|ARBA:ARBA00011165}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC       {ECO:0000256|ARBA:ARBA00007186}.
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:KQN27449.1}.
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DR   EMBL; LMLC01000004; KQN27449.1; -; Genomic_DNA.
DR   RefSeq; WP_055880347.1; NZ_LMLC01000004.1.
DR   AlphaFoldDB; A0A0Q4KT90; -.
DR   OrthoDB; 9758333at2; -.
DR   Proteomes; UP000051932; Unassembled WGS sequence.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR   PANTHER; PTHR43576:SF2; INTRACELLULAR EXO-ALPHA-L-ARABINOFURANOSIDASE 2; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..518
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006224795"
FT   DOMAIN          321..511
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   518 AA;  56829 MW;  9D17793763CB1228 CRC64;
     MRMMFTAIAL VLSSPALAQQ APPVDGAPAA VTVHGDKPAP KFDKRIFGQF AEHLGTGVYG
     GIWVGKGSRI PNVNGYRTDV LDALKAIRTP VIRWPGGCFA DEYHWREGIG APAKRKVKIN
     TNWGGVTEDN AVGTHEFMNY SEMVGAEPYV SGNVGNGTPS EMAEWVEYMT SPTGSSLAKE
     RAANGRKAPW KLPMFGIGNE LWGCGGNMRP EYAADVTRRY STFVKMPEGQ RVMKIASGAN
     ADDYNWTDVM MRDAGAHFDG IGVHYYTIPY DWAKKGAATG FDEDQWARTL AKTVKMDDYI
     TEHAKRMDKY DPGKRVALLV DEWGTWYDQE PGSHPGFLYQ QNSLRDALVT SLNFDIFARH
     TDRLRGANIA QMVNVLQAML LTDGNRMVRT PTYWVFDMYK DYQDGVVLPV DVQSRWYNKN
     QWTLKAVSAS AVRGVDGAVH MGLTNVDPNQ PATVSVKLDG VTGAGITGRI LTASAIDAHN
     TFDAPDVVKP AAFTGATLAN GTLTVTLPPK SVVMLDIR
//
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