ID IABF_STRAW Reviewed; 481 AA.
AC Q82P90;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Extracellular exo-alpha-(1->5)-L-arabinofuranosidase {ECO:0000305|PubMed:18665359};
DE EC=3.2.1.55 {ECO:0000269|PubMed:18665359};
DE Flags: Precursor;
GN Name=Araf43A {ECO:0000303|PubMed:18665359}; Synonyms=abfA;
GN ORFNames=SAVERM_1043;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=18665359; DOI=10.1007/s00253-008-1551-x;
RA Ichinose H., Yoshida M., Fujimoto Z., Kaneko S.;
RT "Characterization of a modular enzyme of exo-1,5-alpha-L-
RT arabinofuranosidase and arabinan binding module from Streptomyces
RT avermitilis NBRC14893.";
RL Appl. Microbiol. Biotechnol. 80:399-408(2008).
RN [4] {ECO:0007744|PDB:3AKF, ECO:0007744|PDB:3AKG, ECO:0007744|PDB:3AKH}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 28-481 IN COMPLEX WITH SUBSTRATE,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-47; ASP-162; ASN-186;
RP TYR-219; GLU-223 AND LEU-316.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=20739278; DOI=10.1074/jbc.m110.164251;
RA Fujimoto Z., Ichinose H., Maehara T., Honda M., Kitaoka M., Kaneko S.;
RT "Crystal structure of an Exo-1,5-{alpha}-L-arabinofuranosidase from
RT Streptomyces avermitilis provides insights into the mechanism of substrate
RT discrimination between exo- and endo-type enzymes in glycoside hydrolase
RT family 43.";
RL J. Biol. Chem. 285:34134-34143(2010).
CC -!- FUNCTION: Involved in the degradation of arabinan and is a key enzyme
CC in the complete degradation of the plant cell wall. Catalyzes only the
CC cleavage of terminal alpha-(1->5) arabinofuranosyl bonds of arabinan
CC present in the arabinofuranosyl polysaccharides or oligosaccharides. It
CC cannot act on other arabinose-containing polysaccharides and
CC arabinoxylo-oligosaccharides. {ECO:0000269|PubMed:18665359}.
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:18665359};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for p-nitrophenyl-alpha-L-arabinofuranoside
CC {ECO:0000269|PubMed:20739278};
CC Note=kcat is 6.5 min(-1) with p-nitrophenyl-alpha-L-arabinofuranoside
CC as substrate. {ECO:0000269|PubMed:20739278};
CC pH dependence:
CC Optimum pH is 6.0. Stable from pH 5.0 to pH 6.5.
CC {ECO:0000269|PubMed:18665359};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:18665359};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000305|PubMed:18665359}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain and
CC a C-terminal arabinose-binding domain (ABD). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 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; BA000030; BAC68753.1; -; Genomic_DNA.
DR PDB; 3AKF; X-ray; 2.20 A; A=28-481.
DR PDB; 3AKG; X-ray; 1.80 A; A=28-481.
DR PDB; 3AKH; X-ray; 1.70 A; A=28-481.
DR PDB; 3AKI; X-ray; 2.00 A; A=28-481.
DR PDBsum; 3AKF; -.
DR PDBsum; 3AKG; -.
DR PDBsum; 3AKH; -.
DR PDBsum; 3AKI; -.
DR AlphaFoldDB; Q82P90; -.
DR SMR; Q82P90; -.
DR KEGG; sma:SAVERM_1043; -.
DR eggNOG; COG3940; Bacteria.
DR HOGENOM; CLU_009397_2_1_11; -.
DR OrthoDB; 177947at2; -.
DR UniPathway; UPA00667; -.
DR EvolutionaryTrace; Q82P90; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0005576; C:extracellular region; 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 CDD; cd18817; GH43f_LbAraf43-like; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF110221; AbfB domain; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..481
FT /note="Extracellular exo-alpha-(1->5)-L-
FT arabinofuranosidase"
FT /id="PRO_5004300134"
FT REGION 37..336
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 349..479
FT /note="ABD"
FT /evidence="ECO:0000255"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:20739278"
FT ACT_SITE 223
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:20739278"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20739278"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20739278"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20739278"
FT BINDING 363..366
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20739278"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20739278"
FT BINDING 457..460
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20739278"
FT BINDING 475
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20739278"
FT SITE 162
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000305|PubMed:20739278"
FT MUTAGEN 47
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20739278"
FT MUTAGEN 47
FT /note="D->N: Maintains an extremely weak catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:20739278"
FT MUTAGEN 162
FT /note="D->A,N: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20739278"
FT MUTAGEN 186
FT /note="N->A,L: Reduces substrate specificity."
FT /evidence="ECO:0000269|PubMed:20739278"
FT MUTAGEN 219
FT /note="Y->A: Reduces substrate specificity and allows
FT hydrolysis of alpha-1,5-linked arabinofuranosyl bonds."
FT /evidence="ECO:0000269|PubMed:20739278"
FT MUTAGEN 223
FT /note="E->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20739278"
FT MUTAGEN 316
FT /note="L->A: Reduces substrate specificity and allows
FT hydrolysis of alpha-1,5-linked arabinofuranosyl bonds."
FT /evidence="ECO:0000269|PubMed:20739278"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:3AKH"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:3AKH"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 183..196
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:3AKH"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:3AKH"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3AKH"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 282..292
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 298..310
FT /evidence="ECO:0007829|PDB:3AKH"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:3AKH"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:3AKH"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:3AKH"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 453..458
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:3AKH"
FT HELIX 470..475
FT /evidence="ECO:0007829|PDB:3AKH"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:3AKH"
SQ SEQUENCE 481 AA; 53105 MW; 61AF442D20B07738 CRC64;
MRRLTVRLFT AVLAALALLT MGTPAHATAP ASPSVTFTNP LAEKRADPHI FKHTDGYYYF
TATVPEYDRI VLRRATTLQG LATAPETTIW TKHASGVMGA HIWAPEIHFI DGKWYVYFAA
GSTSDVWAIR MYVLESGAAN PLTGSWTEKG QIATPVSSFS LDATTFVVNG VRHLAWAQRN
PAEDNNTSLF IAKMANPWTI SGTPTEISQP TLSWETVGYK VNEGPAVIQH GGKVFLTYSA
SATDANYCLG MLSASASADL LNAASWTKSS QPVFKTSEAT GQYGPGHNSF TVSEDGKSDI
LVYHDRNYKD ISGDPLNDPN RRTRLQKVYW NADGTPNFGI PVADGVTPVR FSSYNYPDRY
IRHWDFRARI EANVTNLADS QFRVVTGLAG SGTISLESAN YPGYYLRHKN YEVWVEKNDG
SSAFKNDASF SRRAGLADSA DGIAFESYNY PGRYLRHYEN LLRIQPVSTA LDRQDATFYA
E
//
