ID   IABF_HALH5              Reviewed;         500 AA.
AC   Q9KBR4;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Intracellular exo-alpha-(1->5)-L-arabinofuranosidase;
DE            Short=ABF;
DE            EC=3.2.1.55;
DE   AltName: Full=Intracellular arabinan exo-alpha-(1->5)-L-arabinosidase;
DE            Short=Arabinosidase;
GN   Name=abfA; OrderedLocusNames=BH1861;
OS   Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Halalkalibacterium (ex Joshi et al. 2022).
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Involved in the degradation of arabinan and is a key enzyme
CC       in the complete degradation of the plant cell wall. Catalyzes the
CC       cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different
CC       hemicellulosic homopolysaccharides (branched and debranched arabinans)
CC       (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR   EMBL; BA000004; BAB05580.1; -; Genomic_DNA.
DR   PIR; E83882; E83882.
DR   RefSeq; WP_010898022.1; NC_002570.2.
DR   AlphaFoldDB; Q9KBR4; -.
DR   SMR; Q9KBR4; -.
DR   STRING; 272558.gene:10727759; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   KEGG; bha:BH1861; -.
DR   eggNOG; COG3534; Bacteria.
DR   HOGENOM; CLU_017810_1_1_9; -.
DR   OrthoDB; 9758333at2; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
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   Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..500
FT                   /note="Intracellular exo-alpha-(1->5)-L-
FT                   arabinofuranosidase"
FT                   /id="PRO_0000057699"
FT   ACT_SITE        174
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        293
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173..174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            297
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            350
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   500 AA;  56402 MW;  802337EEA0F225B5 CRC64;
     MTLTATMVVD KSFKIGEIDK RIYGSFIEHL GRAVYEGIYE PGHPDGDEQG FRKDVIRLVQ
     ELQVPLVRYP GGNFVSGYNW EDGVGPVSER PKRLDLAWRT TETNEIGTNE FVDWAKKVGA
     EVNMAVNLGS RGVDAARNLV EYCNHPSGSY WSDLRISHGY KDPHNIKTWC LGNEMDGPWQ
     IGQKTAEEYG RVAAEAGKVM KLVDPSIELV ACGSSNSKMA TFADWEATVL DHTYDYVDYI
     SLHTYYGNRD DDLANYLAQS MDMDEFIRSV IAIADYVKAK KRSKKTIHLS FDEWNVWFHS
     NEADRQITPW SVAPPLLEDI YTFEDALLVG SMLITLLKHA DRVKIACLAQ LVNVIAPIMT
     EKGGPAWKQT IFYPYMHASV YGRGVALQAQ ISSPKYDSKD FTDVPYLDAA VVHLEEAEEV
     TIFAVNKHQT ESLNLQCDMR SFEGYHVLEH IVLEHENMKA TNQGREQVTP HHNGDSAIDQ
     GRLTANLAKL SWNVIRLGKK
//