IABF_STRLI
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 03-AUG-2022, entry version 80.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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 PRIDE; P53627; -.
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; 2.60.40.1180; -; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; SSF51445; 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
