ID IABF_STRLI Reviewed; 662 AA. AC P53627; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 28-JUN-2023, entry version 85. DE RecName: Full=Intracellular exo-alpha-(1->5)-L-arabinofuranosidase; DE Short=ABF; DE EC=3.2.1.55; DE AltName: Full=Alpha-L-AF; DE AltName: Full=Arabinoxylan arabinofuranohydrolase; DE AltName: Full=Intracellular arabinan exo-alpha-(1->5)-L-arabinosidase; DE Short=Arabinosidase; GN Name=abfA; OS Streptomyces lividans. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1916; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23, FUNCTION, RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, RP SUBSTRATE SPECIFICITY, AND SUBUNIT. RC STRAIN=66 / 1326; RX PubMed=8092996; DOI=10.1042/bj3020443; RA Manin C., Shareek F., Morosoli R., Kluepfel D.; RT "Purification and characterization of an alpha-L-arabinofuranosidase from RT Streptomyces lividans 66 and DNA sequence of the gene (abfA)."; RL Biochem. J. 302:443-449(1994). 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 (arabino-oligoxylosides, branched CC and debranched arabinans). It acts rapidly on the short-chain arabino- CC oligoxylosides from digestion of xylan with xylanases. It hydrolyzes CC slowly arabinan and arabinoxylan from wheat and rye flour. CC {ECO:0000269|PubMed:8092996}. 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:0000269|PubMed:8092996}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.6 mM for p-nitrophenyl alpha-L-arabinofuranoside (pNP-Araf) (at CC 60 degrees Celsius and at pH 6) {ECO:0000269|PubMed:8092996}; CC Vmax=180 umol/min/mg enzyme (at 60 degrees Celsius and at pH 6) CC {ECO:0000269|PubMed:8092996}; CC pH dependence: CC Optimum pH is 6.0. {ECO:0000269|PubMed:8092996}; CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius. CC {ECO:0000269|PubMed:8092996}; CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation. CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000305|PubMed:8092996}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8092996}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U04630; AAA61708.1; -; Genomic_DNA. DR PIR; S55274; S55274. DR AlphaFoldDB; P53627; -. DR SMR; P53627; -. DR CAZy; GH51; Glycoside Hydrolase Family 51. DR BRENDA; 3.2.1.55; 6052. DR UniPathway; UPA00667; -. 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 1: Evidence at protein level; KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Glycosidase; KW Hydrolase. FT CHAIN 1..662 FT /note="Intracellular exo-alpha-(1->5)-L- FT arabinofuranosidase" FT /id="PRO_0000057704" FT REGION 454..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 497..548 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 588..662 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 599..623 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 646..662 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 175 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 294 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 27 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 72 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 174..175 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 246 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 294 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 352 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 298 FT /note="Important for substrate recognition" FT /evidence="ECO:0000250" FT SITE 352 FT /note="Important for substrate recognition" FT /evidence="ECO:0000250" SQ SEQUENCE 662 AA; 72497 MW; DAAF66A577C1D6D1 CRC64; MRTARFTLDP AFTVGAVNPR LFGSFVEHLG RCVYTGVFEP GHPTADAEGL RQDVLELVRE LGVTAVRYPG GNFVSGYKWE DSVGPVEDRP RRLDLAWRST ETNRFGLSEY IAFLKKIGPQ AEPMMAVNLG TRGVAEALEL QEYANHPSGT ALSDLRAEHG DKDPFGIRLW CLGNEMDGPW QTGHKTAEEY GRVAAETARA MRQIDPDVEL VACGSSGQSM ETFAEWEATV LKETYDLVDH ISLHAYYEPH DGDVDSFLAS AVDMESFIEN VVATCDHVGA RLKSKKKINL SFDEWNVWYM TKTQAEVSAL DWPEAPRLLE DNYSVMDAVV FGSLLIALLR HADRVTVACL AQLVNVIAPI MTEPGGPAWR QTTFFPFSQA SKYGRGEVLD VRVDSPTYDT AKYGEADLLH ATAVVRARRS VTVFAVNRSR TGALPLEVAL SGLELTEVVE HSALADADPD ARNTLAEPER VVPHPVDGTS LRDGRLTAAL EPLSWNSIRC ADPAPGQPPR RPGEGTGFTG TPPAAPPSSS SAPRPDPTAR RSPDRTARAR VLAAARVRRM PFGRTKVCGA PVRPPTYAPR FQPFRKTWTR WAPAPRSGSP SRRSPTEASI PGGTSSRNVV RYQVTPWRRS PPGSAPGTPA PTRRRRTRAG ASRGAPRTAR RC //