ARBA_CELJU
ID ARBA_CELJU Reviewed; 347 AA.
AC P95470;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA;
DE Short=ABF;
DE EC=3.2.1.55 {ECO:0000269|PubMed:15708971, ECO:0000269|PubMed:9163351};
DE AltName: Full=Extracellular arabinan exo-alpha-(1->5)-L-arabinosidase ArbA;
DE Short=Arabinosidase;
DE Flags: Precursor;
GN Name=arbA;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-51, FUNCTION,
RP CATALYTIC ACTIVITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=9163351; DOI=10.1042/bj3230547;
RA McKie V.A., Black G.W., Millward-Sadler S.J., Hazlewood G.P., Laurie J.I.,
RA Gilbert H.J.;
RT "Arabinanase A from Pseudomonas fluorescens subsp. cellulosa exhibits both
RT an endo- and an exo- mode of action.";
RL Biochem. J. 323:547-555(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-35; PRO-55 AND GLN-316,
RP AND REACTION MECHANISM.
RX PubMed=15708971; DOI=10.1073/pnas.0500051102;
RA Proctor M.R., Taylor E.J., Nurizzo D., Turkenburg J.P., Lloyd R.M.,
RA Vardakou M., Davies G.J., Gilbert H.J.;
RT "Tailored catalysts for plant cell-wall degradation: redesigning the
RT exo/endo preference of Cellvibrio japonicus arabinanase 43A.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2697-2702(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 30-347 OF MUTANT ALA-158 IN
RP COMPLEX WITH ALPHA-L-ARABINOFURANOSE, FUNCTION, MUTAGENESIS OF ASP-38;
RP PHE-114; ASP-158 AND GLU-221, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=12198486; DOI=10.1038/nsb835;
RA Nurizzo D., Turkenburg J.P., Charnock S.J., Roberts S.M., Dodson E.J.,
RA McKie V.A., Taylor E.J., Gilbert H.J., Davies G.J.;
RT "Cellvibrio japonicus alpha-L-arabinanase 43A has a novel five-blade beta-
RT propeller fold.";
RL Nat. Struct. Biol. 9:665-668(2002).
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 the terminal alpha-(1->5)-arabinofuranosyl bonds of linear
CC arabinan and carboxymethylarabinan to produce almost exclusively
CC arabinotriose. {ECO:0000269|PubMed:12198486,
CC ECO:0000269|PubMed:15708971, ECO:0000269|PubMed:9163351}.
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:15708971, ECO:0000269|PubMed:9163351};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 mM for arabinan {ECO:0000269|PubMed:12198486,
CC ECO:0000269|PubMed:9163351};
CC KM=3.75 mM for arabinan {ECO:0000269|PubMed:12198486,
CC ECO:0000269|PubMed:9163351};
CC Note=kcat is 17.1 sec(-1) for arabinan. kcat is 212 sec(-1) for
CC carboxymethylarabinan.;
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12198486}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:9163351}.
CC -!- INDUCTION: Induced by arabinan and repressed by glucose.
CC {ECO:0000269|PubMed:9163351}.
CC -!- MISCELLANEOUS: The relative activity of the enzyme against the arabino-
CC oligosaccharides increases with the increasing size of the substrate up
CC to arabinohexaose, after which the rate remains constant. The
CC substrate-binding site accommodates six arabinose units, with cleavage
CC occurring between binding sites 3 and 4 (PubMed:9163351).
CC {ECO:0000305|PubMed:9163351}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; Y10458; CAA71485.1; -; Genomic_DNA.
DR PDB; 1GYD; X-ray; 2.05 A; B=33-347.
DR PDB; 1GYE; X-ray; 2.50 A; B=32-346.
DR PDB; 1GYH; X-ray; 1.89 A; A/B/C/D/E/F=30-347.
DR PDBsum; 1GYD; -.
DR PDBsum; 1GYE; -.
DR PDBsum; 1GYH; -.
DR AlphaFoldDB; P95470; -.
DR SMR; P95470; -.
DR STRING; 498211.CJA_0805; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR eggNOG; COG3507; Bacteria.
DR UniPathway; UPA00667; -.
DR EvolutionaryTrace; P95470; -.
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:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:InterPro.
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; Direct protein sequencing;
KW Glycosidase; Hydrolase; Metal-binding; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:9163351"
FT CHAIN 32..347
FT /note="Extracellular exo-alpha-(1->5)-L-arabinofuranosidase
FT ArbA"
FT /id="PRO_0000422121"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:12198486"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12198486"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12198486"
FT BINDING 90..92
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12198486"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12198486"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12198486"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12198486"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12198486"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12198486"
FT SITE 158
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:12198486"
FT SITE 291
FT /note="Important for substrate recognition and
FT stabilization"
FT MUTAGEN 35
FT /note="D->L: Very slight decrease in exo-
FT arabinofuranosidase activity. Switch from exo to an endo
FT mode of action."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 38
FT /note="D->A: Loss of arabinofuranosidase activity."
FT /evidence="ECO:0000269|PubMed:12198486"
FT MUTAGEN 38
FT /note="D->E: Strong decrease of binding affinity."
FT /evidence="ECO:0000269|PubMed:12198486"
FT MUTAGEN 38
FT /note="D->N: Slight decrease of binding affinity."
FT /evidence="ECO:0000269|PubMed:12198486"
FT MUTAGEN 55
FT /note="P->LTEER: 130-fold less active than wild-type."
FT /evidence="ECO:0000269|PubMed:15708971"
FT MUTAGEN 114
FT /note="F->A: Strong decrease of binding affinity."
FT /evidence="ECO:0000269|PubMed:12198486"
FT MUTAGEN 158
FT /note="D->A: Loss of arabinofuranosidase activity."
FT /evidence="ECO:0000269|PubMed:12198486"
FT MUTAGEN 158
FT /note="D->N: Loss of arabinofuranosidase activity."
FT /evidence="ECO:0000269|PubMed:12198486"
FT MUTAGEN 221
FT /note="E->A: Loss of arabinofuranosidase activity."
FT /evidence="ECO:0000269|PubMed:12198486"
FT MUTAGEN 221
FT /note="E->Q: Loss of arabinofuranosidase activity."
FT /evidence="ECO:0000269|PubMed:12198486"
FT MUTAGEN 316
FT /note="Q->L: Very slight decrease in arabinofuranosidase
FT activity."
FT /evidence="ECO:0000269|PubMed:15708971"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 58..77
FT /evidence="ECO:0007829|PDB:1GYH"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:1GYH"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:1GYH"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1GYH"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 284..297
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:1GYH"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:1GYH"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:1GYH"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:1GYE"
SQ SEQUENCE 347 AA; 39432 MW; C0171992B6F8C314 CRC64;
MPTHHPITRQ HWHHSWLSAL ALLCASLACG AKQVDVHDPV MTREGDTWYL FSTGPGITIY
SSKDRVNWRY SDRAFGTEPT WAKRVSPSFD GHLWAPDIYQ HKGLFYLYYS VSAFGKNTSA
IGVTVNKTLN PASPDYRWED KGIVIESVPQ RDLWNAIDPA IIADDHGQVW MSFGSFWGGL
KLFKLNDDLT RPAEPQEWHS IAKLERSVLM DDSQAGSAQI EAPFILRKGD YYYLFASWGL
CCRKGDSTYH LVVGRSKQVT GPYLDKTGRD MNQGGGSLLI KGNKRWVGLG HNSAYTWDGK
DYLVLHAYEA ADNYLQKLKI LNLHWDGEGW PQVDEKELDS YISQRLK
