REX8A_PAEBA
ID REX8A_PAEBA Reviewed; 380 AA.
AC A0A0S2UQQ5;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Reducing-end xylose-releasing exo-oligoxylanase Rex8A {ECO:0000303|PubMed:27316951};
DE Short=Rex {ECO:0000303|PubMed:27316951};
DE EC=3.2.1.156 {ECO:0000269|PubMed:27316951};
GN Name=rex8A {ECO:0000303|PubMed:27316951, ECO:0000312|EMBL:ALP73600.1};
GN ORFNames=DFQ00_11062 {ECO:0000312|EMBL:PYE48000.1};
OS Paenibacillus barcinonensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=198119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, PATHWAY, 3D-STRUCTURE
RP MODELING, ACTIVE SITE, AND MUTAGENESIS OF GLU-70.
RC STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX PubMed=27316951; DOI=10.1128/aem.01329-16;
RA Valenzuela S.V., Lopez S., Biely P., Sanz-Aparicio J., Pastor F.I.;
RT "The glycoside hydrolase family 8 reducing-end xylose-releasing exo-
RT oligoxylanase Rex8A from Paenibacillus barcinonensis BP-23 is active on
RT branched xylooligosaccharides.";
RL Appl. Environ. Microbiol. 82:5116-5124(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX PubMed=26203337; DOI=10.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
CC -!- FUNCTION: Involved in depolymerization of xylan, a major component of
CC the lignocellulosic substrates. Acts as an exo-oligoxylanase that
CC efficiently hydrolyzes xylooligosaccharides, releasing xylose from
CC their reducing ends. Hydrolyzes xylooligomers of 3 to 6 xylose units to
CC xylose and xylobiose. Besides linear xylooligosaccharides, also
CC hydrolyzes branched xylooligomers, such as xylooligomers decorated with
CC 4-O-methyl-D-glucuronic acid moieties. Its proposed role is the
CC degradation of xylooligomers produced by the activity of extracellular
CC xylanases once they have been transported inside cells. Shows minor
CC activity on polymeric xylan (glucuronoxylan from beechwood). Is not
CC active on cellooligosaccharides or cellulosic substrates, or on other
CC polysaccharides such as pectin, polygalacturonic acid, laminarin, or
CC lichenan. {ECO:0000269|PubMed:27316951}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylose residues from the reducing
CC end of oligosaccharides.; EC=3.2.1.156;
CC Evidence={ECO:0000269|PubMed:27316951};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.64 mM for xylotriose {ECO:0000269|PubMed:27316951};
CC Vmax=152.2 umol/min/mg enzyme for the hydrolysis of xylotriose
CC {ECO:0000269|PubMed:27316951};
CC Note=kcat is 118.8 sec(-1) for the hydrolysis of xylotriose.
CC {ECO:0000269|PubMed:27316951};
CC pH dependence:
CC Optimum pH is 7 for the hydrolysis of xylotriose.
CC {ECO:0000269|PubMed:27316951};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius for the hydrolysis of
CC xylotriose. {ECO:0000269|PubMed:27316951};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000269|PubMed:27316951}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC {ECO:0000305}.
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DR EMBL; KT251207; ALP73600.1; -; Genomic_DNA.
DR EMBL; QJSW01000010; PYE48000.1; -; Genomic_DNA.
DR PDB; 6SHY; X-ray; 1.81 A; A/B=1-380.
DR PDB; 6SRD; X-ray; 1.93 A; A/B=1-380.
DR PDB; 6SUD; X-ray; 1.74 A; A/B=1-380.
DR PDB; 6TO0; X-ray; 1.88 A; A/B=1-380.
DR PDB; 6TOW; X-ray; 2.05 A; A/B=1-380.
DR PDB; 6TPP; X-ray; 2.64 A; A/B=1-380.
DR PDB; 6TRH; X-ray; 1.86 A; A/B/C/D=1-380.
DR PDBsum; 6SHY; -.
DR PDBsum; 6SRD; -.
DR PDBsum; 6SUD; -.
DR PDBsum; 6TO0; -.
DR PDBsum; 6TOW; -.
DR PDBsum; 6TPP; -.
DR PDBsum; 6TRH; -.
DR AlphaFoldDB; A0A0S2UQQ5; -.
DR SMR; A0A0S2UQQ5; -.
DR EnsemblBacteria; PYE48000; PYE48000; DFQ00_11062.
DR BRENDA; 3.2.1.156; 13889.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000247790; Unassembled WGS sequence.
DR GO; GO:0033951; F:oligosaccharide reducing-end xylanase activity; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR002037; Glyco_hydro_8.
DR Pfam; PF01270; Glyco_hydro_8; 1.
DR PRINTS; PR00735; GLHYDRLASE8.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..380
FT /note="Reducing-end xylose-releasing exo-oligoxylanase
FT Rex8A"
FT /id="PRO_0000446222"
FT ACT_SITE 70
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27316951"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27316951"
FT MUTAGEN 70
FT /note="E->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:27316951"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:6SUD"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6SUD"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6SUD"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6SUD"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 153..170
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6SHY"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6SRD"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:6TRH"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 215..232
FT /evidence="ECO:0007829|PDB:6SUD"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6SUD"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:6SUD"
FT HELIX 359..373
FT /evidence="ECO:0007829|PDB:6SUD"
SQ SEQUENCE 380 AA; 44217 MW; 4AF704EE56FE61F9 CRC64;
MNITGKGAYD TGTYANLFQR SGYREDEIKA RLEQTWNDLF YGDEHTRIYY PVGDDKGYML
DTGNDDVRSE GMSYGMMMAV QMDKKHEFDR LWNYAYTYMQ HTEGRYKDYF AWHCKPDGTR
LSPGPAPDGE EFFAMALFFA SNRWGDGPAP YDYQAQARKI LHACLHQGEQ GEGDPMWEPS
NRLIKFIPEL PFSDPSYHLP HFYELFAQYA NEQDRTFWKE AAEASRAYLR TACHPVTGLS
PEYANYDGTP APVQLHGDFR HFYSDAYRVA ANVALDWEWF RKDPWQVQQS NRIQAFFSDI
DVSDYRRYTI EGEPFNEPAL HPVGLLATNA MASLAADGPD ADSFVKRFWN TPLRQGKRRY
YDNCLYFFTM LALSGNYRVY
