IABF_ACET2
ID IABF_ACET2 Reviewed; 503 AA.
AC A3DIH0;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 OrderedLocusNames=Cthe_2548;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-173, ACTIVE SITE,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=16336192; DOI=10.1042/bj20051780;
RA Taylor E.J., Smith N.L., Turkenburg J.P., D'Souza S., Gilbert H.J.,
RA Davies G.J.;
RT "Structural insight into the ligand specificity of a thermostable family 51
RT arabinofuranosidase, Araf51, from Clostridium thermocellum.";
RL Biochem. J. 395:31-37(2006).
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 small
CC oligosaccharides as alpha-(1->5)-linked arabinobiose/arabinotriose, but
CC does not display significant activity against linear non-substituted
CC arabinan. It is also highly efficient in the cleavage of alpha-(1->3)-
CC linked arabinoside of xylobiose and of the alpha-(1->3)-linked
CC arabinoside decorations of polymeric wheat arabinoxylan. It exhibits
CC very low activity against sugar beet arabinan.
CC {ECO:0000269|PubMed:16336192}.
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:16336192};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.5 uM for wheat arabinoxylan (at 37 degrees Celsius and at pH 7)
CC {ECO:0000269|PubMed:16336192};
CC KM=0.25 mM for p-nitrophenyl alpha-L-arabinofuranoside (pNP-Araf)(at
CC 37 degrees Celsius and at pH 7) {ECO:0000269|PubMed:16336192};
CC KM=0.55 mM for alpha-(1->5)-linked arabinotriose (at 37 degrees
CC Celsius and at pH 7) {ECO:0000269|PubMed:16336192};
CC KM=0.95 mM for alpha-(1->3)-linked arabinoside of xylobiose (at 37
CC degrees Celsius and at pH 7) {ECO:0000269|PubMed:16336192};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:16336192};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:16336192};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000269|PubMed:16336192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16336192}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR EMBL; CP000568; ABN53749.1; -; Genomic_DNA.
DR PDB; 2C7F; X-ray; 2.70 A; A/B/C/D/E/F=1-503.
DR PDB; 2C8N; X-ray; 2.90 A; A/B/C/D/E/F=1-503.
DR PDB; 5O7Z; X-ray; 2.64 A; A/B/C/D/E/F=2-502.
DR PDB; 5O80; X-ray; 2.92 A; A/B/C/D/E/F=2-502.
DR PDB; 5O81; X-ray; 2.50 A; A/B/C/D/E/F=2-502.
DR PDB; 5O82; X-ray; 2.39 A; A/B/C/D/E/F=2-502.
DR PDBsum; 2C7F; -.
DR PDBsum; 2C8N; -.
DR PDBsum; 5O7Z; -.
DR PDBsum; 5O80; -.
DR PDBsum; 5O81; -.
DR PDBsum; 5O82; -.
DR AlphaFoldDB; A3DIH0; -.
DR SMR; A3DIH0; -.
DR STRING; 203119.Cthe_2548; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR EnsemblBacteria; ABN53749; ABN53749; Cthe_2548.
DR KEGG; cth:Cthe_2548; -.
DR eggNOG; COG3534; Bacteria.
DR HOGENOM; CLU_017810_1_1_9; -.
DR OMA; SKYMRGW; -.
DR OrthoDB; 620389at2; -.
DR BRENDA; 3.2.1.55; 1530.
DR UniPathway; UPA00667; -.
DR EvolutionaryTrace; A3DIH0; -.
DR Proteomes; UP000002145; 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; 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 3D-structure; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..503
FT /note="Intracellular exo-alpha-(1->5)-L-
FT arabinofuranosidase"
FT /id="PRO_0000422128"
FT ACT_SITE 173
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:16336192"
FT ACT_SITE 292
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:16336192"
FT BINDING 27
FT /ligand="substrate"
FT BINDING 72
FT /ligand="substrate"
FT BINDING 172..173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="substrate"
FT BINDING 292
FT /ligand="substrate"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 296
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 352
FT /note="Important for substrate recognition"
FT MUTAGEN 173
FT /note="E->A: Absence of arabinofuranosidase activity."
FT /evidence="ECO:0000269|PubMed:16336192"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5O82"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5O7Z"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5O82"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 185..202
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:5O82"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 259..280
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:5O82"
FT TURN 341..344
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5O82"
FT HELIX 375..384
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 405..417
FT /evidence="ECO:0007829|PDB:5O82"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:5O81"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:5O80"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:5O80"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:2C8N"
FT STRAND 484..491
FT /evidence="ECO:0007829|PDB:5O82"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:5O82"
SQ SEQUENCE 503 AA; 57701 MW; 7F030C55B69BF17E CRC64;
MKKARMTVDK DYKIAEIDKR IYGSFVEHLG RAVYDGLYQP GNSKSDEDGF RKDVIELVKE
LNVPIIRYPG GNFVSNYFWE DGVGPVEDRP RRLDLAWKSI EPNQVGINEF AKWCKKVNAE
IMMAVNLGTR GISDACNLLE YCNHPGGSKY SDMRIKHGVK EPHNIKVWCL GNEMDGPWQV
GHKTMDEYGR IAEETARAMK MIDPSIELVA CGSSSKDMPT FPQWEATVLD YAYDYVDYIS
LHQYYGNKEN DTADFLAKSD DLDDFIRSVI ATCDYIKAKK RSKKDIYLSF DEWNVWYHSN
NEDANIMQNE PWRIAPPLLE DIYTFEDALL VGLMLITLMK HADRIKIACL AQLINVIAPI
VTERNGGAAW RQTIFYPFMH ASKYGRGIVL QPVINSPLHD TSKHEDVTDI ESVAIYNEEK
EEVTIFAVNR NIHEDIVLVS DVRGMKDYRL LEHIVLEHQD LKIRNSVNGE EVYPKNSDKS
SFDDGILTSM LRRASWNVIR IGK
