ID   E1V3J7_HALED            Unreviewed;       508 AA.
AC   E1V3J7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Alpha-L-arabinofuranosidase {ECO:0000313|EMBL:CBV42676.1};
DE            EC=3.2.1.55 {ECO:0000313|EMBL:CBV42676.1};
GN   Name=abfA {ECO:0000313|EMBL:CBV42676.1};
GN   OrderedLocusNames=HELO_2792 {ECO:0000313|EMBL:CBV42676.1};
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV42676.1, ECO:0000313|Proteomes:UP000008707};
RN   [1] {ECO:0000313|Proteomes:UP000008707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC   {ECO:0000313|Proteomes:UP000008707};
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
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}.
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DR   EMBL; FN869568; CBV42676.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1V3J7; -.
DR   STRING; 768066.HELO_2792; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   KEGG; hel:HELO_2792; -.
DR   eggNOG; COG3534; Bacteria.
DR   HOGENOM; CLU_017810_1_1_6; -.
DR   OrthoDB; 9758333at2; -.
DR   Proteomes; UP000008707; Chromosome.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
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:SF3; ALPHA-L-ARABINOFURANOSIDASE C; 1.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 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   Glycosidase {ECO:0000313|EMBL:CBV42676.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBV42676.1}.
FT   DOMAIN          290..494
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   508 AA;  57751 MW;  BB29FDFDF13190B5 CRC64;
     MLIRASLHRD FKISTIDDRL YSAFIEHMGR AIYSGIYEPG HPEADSNGFR LDVLELVRAL
     NIPAIRYPGG NFVSAYRWED GVGPKDQRPV RLDLAWRSKE TNQVGINEFA QWAEMAGIDM
     MLAVNLGSRG LEDARNFAEY VLHPSGTYWS DLRRSHDVNK PYDVRMWCLG NEMDGPWQVG
     QKNAREYGHL ANETSKALKA INGNIEAIVC GSSNDEMPTY PDWEREVLEE CYENVDYISL
     HKYFGNSSND TLNYFGKIEE TGRYIQAIGG VIDFVKAKKR AKNDIYICFD EWNVWYHQRE
     EDSRRWQTWD WPEAPDLLEE DYNFEDALFV AGLLNEFIRR SDRVRIACIA QLVNVIAPIR
     AEKGGIAWCQ TIYYPYQFAS LYGRGVALNV SVDGPTYDCS VADDVNYLDV AAVHDEKSEK
     VTLFLVNRHL EETADLDLSL YGFDAARVIE HKVMEGFDLR ETNGPNKPSA VSPFDGVGVG
     VEGCQVRGKL SPLSYHVVRL DVGRGARS
//