XYNB_THESA
ID XYNB_THESA Reviewed; 500 AA.
AC P36906;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Beta-xylosidase;
DE EC=3.2.1.37;
DE AltName: Full=1,4-beta-D-xylan xylohydrolase;
DE AltName: Full=Xylan 1,4-beta-xylosidase;
GN Name=xynB;
OS Thermoanaerobacterium saccharolyticum.
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX NCBI_TaxID=28896;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49915 / DSM 7060 / B6A-RI;
RX PubMed=8360617; DOI=10.1099/00221287-139-6-1235;
RA Lee Y.E., Zeikus J.G.;
RT "Genetic organization, sequence and biochemical characterization of
RT recombinant beta-xylosidase from Thermoanaerobacterium saccharolyticum
RT strain B6A-RI.";
RL J. Gen. Microbiol. 139:1235-1243(1993).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 49915 / DSM 7060 / B6A-RI;
RX PubMed=8612648; DOI=10.1111/j.1432-1033.1996.00706.x;
RA Armand S., Vieille C., Gey C., Heyraud A., Zeikus J.G., Henrissat B.;
RT "Stereochemical course and reaction products of the action of beta-
RT xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI.";
RL Eur. J. Biochem. 236:706-713(1996).
RN [3]
RP ACTIVE SITE GLU-277, AND MASS SPECTROMETRY.
RX PubMed=9761746; DOI=10.1042/bj3350449;
RA Vocadlo D.J., MacKenzie L.F., He S., Zeikus G.J., Withers S.G.;
RT "Identification of Glu-277 as the catalytic nucleophile of
RT Thermoanaerobacterium saccharolyticum beta-xylosidase using electrospray
RT MS.";
RL Biochem. J. 335:449-455(1998).
CC -!- FUNCTION: Has hydrolytic activity towards xylopentaose, xylotriose,
CC xylobiose and P-nitrophenyl-beta-D-xylopyranoside, but has no activity
CC toward xylan.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Loses activity at 85
CC degrees Celsius.;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- INDUCTION: By xylan and xylose.
CC -!- MASS SPECTROMETRY: Mass=58666; Mass_error=6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9761746};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 39 family. {ECO:0000305}.
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DR EMBL; M97883; AAA27369.1; -; Genomic_DNA.
DR PIR; S41859; S41859.
DR PDB; 1PX8; X-ray; 2.40 A; A/B=1-500.
DR PDB; 1UHV; X-ray; 2.10 A; A/B/C/D=1-500.
DR PDBsum; 1PX8; -.
DR PDBsum; 1UHV; -.
DR AlphaFoldDB; P36906; -.
DR SMR; P36906; -.
DR BindingDB; P36906; -.
DR ChEMBL; CHEMBL4658; -.
DR CAZy; GH39; Glycoside Hydrolase Family 39.
DR SABIO-RK; P36906; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P36906; -.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000514; Glyco_hydro_39.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01229; Glyco_hydro_39; 1.
DR PRINTS; PR00745; GLHYDRLASE39.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01027; GLYCOSYL_HYDROL_F39; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..500
FT /note="Beta-xylosidase"
FT /id="PRO_0000057689"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10068"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:9761746"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1UHV"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1UHV"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1UHV"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 127..145
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1UHV"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 172..189
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1UHV"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 346..354
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 395..402
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 404..420
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:1UHV"
FT STRAND 473..481
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1UHV"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:1UHV"
SQ SEQUENCE 500 AA; 58606 MW; 3B6D59E70A5F4CBC CRC64;
MIKVRVPDFS DKKFSDRWRY CVGTGRLGLA LQKEYIETLK YVKENIDFKY IRGHGLLCDD
VGIYREDVVG DEVKPFYNFT YIDRIFDSFL EIGIRPFVEI GFMPKKLASG TQTVFYWEGN
VTPPKDYEKW SDLVKAVLHH FISRYGIEEV LKWPFEIWNE PNLKEFWKDA DEKEYFKLYK
VTAKAIKEVN ENLKVGGPAI CGGADYWIED FLNFCYEENV PVDFVSRHAT TSKQGEYTPH
LIYQEIMPSE YMLNEFKTVR EIIKNSHFPN LPFHITEYNT SYSPQNPVHD TPFNAAYIAR
ILSEGGDYVD SFSYWTFSDV FEERDVPRSQ FHGGFGLVAL NMIPKPTFYT FKFFNAMGEE
MLYRDEHMLV TRRDDGSVAL IAWNEVMDKT ENPDEDYEVE IPVRFRDVFI KRQLIDEEHG
NPWGTWIHMG RPRYPSKEQV NTLREVAKPE IMTSQPVAND GYLNLKFKLG KNAVVLYELT
ERIDESSTYI GLDDSKINGY
