IABN_GEOTD
ID IABN_GEOTD Reviewed; 313 AA.
AC Q93HT9;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Intracellular endo-alpha-(1->5)-L-arabinanase;
DE Short=ABN;
DE EC=3.2.1.99;
DE AltName: Full=Endo-1,5-alpha-L-arabinanase;
GN Name=abn-ts;
OS Geobacillus thermodenitrificans.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=33940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=TS-3;
RX PubMed=11999422; DOI=10.1271/bbb.66.430;
RA Takao M., Yamaguchi A., Yoshikawa K., Terashita T., Sakai T.;
RT "Molecular cloning of the gene encoding thermostable endo-1,5-alpha-L-
RT arabinase of Bacillus thermodenitrificans TS-3 and its expression in
RT Bacillus subtilis.";
RL Biosci. Biotechnol. Biochem. 66:430-433(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-313 IN COMPLEX WITH CALCIUM
RP ION, MUTAGENESIS, COFACTOR, AND THERMOSTABILITY.
RX PubMed=15944411; DOI=10.1093/jb/mvi078;
RA Yamaguchi A., Tada T., Wada K., Nakaniwa T., Kitatani T., Sogabe Y.,
RA Takao M., Sakai T., Nishimura K.;
RT "Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from
RT Bacillus thermodenitrificans TS-3.";
RL J. Biochem. 137:587-592(2005).
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 endo alpha-(1->5)-L-arabinofuranosyl residues in debranched
CC arabinan. {ECO:0000269|PubMed:11999422}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC (1->5)-arabinans.; EC=3.2.1.99;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. The enzyme is stable for
CC 30 minutes at temperatures up to 70 degrees Celsius.
CC {ECO:0000269|PubMed:11999422};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The N-terminal 16 amino acids plays an important role in
CC the thermostability. {ECO:0000305|PubMed:15944411}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; AB061269; BAB64339.1; -; Genomic_DNA.
DR PIR; JC7817; JC7817.
DR PDB; 1WL7; X-ray; 1.90 A; A=2-313.
DR PDB; 6A8H; X-ray; 1.65 A; A=1-313.
DR PDB; 6A8I; X-ray; 1.90 A; A/B=1-313.
DR PDBsum; 1WL7; -.
DR PDBsum; 6A8H; -.
DR PDBsum; 6A8I; -.
DR AlphaFoldDB; Q93HT9; -.
DR SMR; Q93HT9; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR BRENDA; 3.2.1.99; 705.
DR UniPathway; UPA00667; -.
DR EvolutionaryTrace; Q93HT9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding.
FT CHAIN 1..313
FT /note="Intracellular endo-alpha-(1->5)-L-arabinanase"
FT /id="PRO_0000422130"
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15944411"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15944411"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT BINDING 144..147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT SITE 147
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:15944411"
FT SITE 271
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000250"
FT MUTAGEN 2..17
FT /note="Missing: No activity is found after 5 minutes at 70
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15944411"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 46..63
FT /evidence="ECO:0007829|PDB:6A8H"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:6A8H"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:6A8H"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:6A8H"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 264..277
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 280..289
FT /evidence="ECO:0007829|PDB:6A8H"
FT TURN 290..294
FT /evidence="ECO:0007829|PDB:6A8H"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:6A8H"
SQ SEQUENCE 313 AA; 35457 MW; 5AA483062433C1DC CRC64;
MVHFHPFGNV NFYEMDWSLK GDLWAHDPVI AKEGSRWYVF HTGSGIQIKT SEDGVHWENM
GRVFPSLPDW CKQYVPEKDE DHLWAPDICF YNGIYYLYYS VSTFGKNTSV IGLATNRTLD
PRDPDYEWKD MGPVIHSTAS DNYNAIDPNV VFDQEGQPWL SFGSFWSGIQ LIQLDTETMK
PAAQAELLTI ASRGEEPNAI EAPFIVCRNG YYYLFVSFDF CCRGIESTYK IAVGRSKDIT
GPYVDKNGVS MMQGGGTILD AGNDRWIGPG HCAVYFSGVS AILVNHAYDA LKNGEPTLQI
RPLYWDDEGW PYL
