XYNC_BACSU
ID XYNC_BACSU Reviewed; 422 AA.
AC Q45070; Q796G4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glucuronoxylanase XynC;
DE EC=3.2.1.136;
DE AltName: Full=Endoxylanase XynC;
DE AltName: Full=Glucuronoxylan xylanohydrolase;
DE Flags: Precursor;
GN Name=xynC; Synonyms=ynfF; OrderedLocusNames=BSU18150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969507; DOI=10.1099/13500872-142-11-3097;
RA Rose M., Entian K.-D.;
RT "New genes in the 170 degrees region of the Bacillus subtilis genome encode
RT DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid
RT transporter.";
RL Microbiology 142:3097-3101(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=15187182; DOI=10.1128/mmbr.68.2.207-233.2004;
RA Tjalsma H., Antelmann H., Jongbloed J.D.H., Braun P.G., Darmon E.,
RA Dorenbos R., Dubois J.-Y.F., Westers H., Zanen G., Quax W.J., Kuipers O.P.,
RA Bron S., Hecker M., van Dijl J.M.;
RT "Proteomics of protein secretion by Bacillus subtilis: separating the
RT 'secrets' of the secretome.";
RL Microbiol. Mol. Biol. Rev. 68:207-233(2004).
RN [4]
RP FUNCTION, INDUCTION, CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168;
RX PubMed=17028274; DOI=10.1128/jb.01283-06;
RA St John F.J., Rice J.D., Preston J.F.;
RT "Characterization of xynC from Bacillus subtilis subsp. subtilis strain 168
RT and analysis of its role in depolymerization of glucuronoxylan.";
RL J. Bacteriol. 188:8617-8626(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS).
RX PubMed=19407387; DOI=10.1107/s1744309109013098;
RA St John F.J., Godwin D.K., Preston J.F., Pozharski E., Hurlbert J.C.;
RT "Crystallization and crystallographic analysis of Bacillus subtilis
RT xylanase C.";
RL Acta Crystallogr. F 65:499-503(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP ACTIVE SITE.
RX PubMed=21256135; DOI=10.1016/j.jmb.2011.01.010;
RA St John F.J., Hurlbert J.C., Rice J.D., Preston J.F., Pozharski E.;
RT "Ligand bound structures of a glycosyl hydrolase family 30 glucuronoxylan
RT xylanohydrolase.";
RL J. Mol. Biol. 407:92-109(2011).
CC -!- FUNCTION: Catalyzes the depolymerization of methylglucuronoxylan
CC (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond
CC penultimate to that linking carbon one of the xylose residue
CC substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).
CC {ECO:0000269|PubMed:17028274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosyl links in some
CC glucuronoarabinoxylans.; EC=3.2.1.136;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=59.5 umol/min/mg enzyme with methylglucuronoxylan from sweetgum
CC as substrate (at 37 degrees Celsius and pH 6)
CC {ECO:0000269|PubMed:17028274};
CC Note=The Km value for methylglucuronoxylan from sweetgum is 1.63
CC mg/ml. The activity is directly correlated to the degree of
CC substitution of the glucuronosyl moiety on the xylan chain.;
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:17028274};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Half the activity is
CC retained for 25 hours at 40 degrees Celsius and for 5 hours at 50
CC degrees Celsius. {ECO:0000269|PubMed:17028274};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15187182}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:17028274}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z73234; CAA97612.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13698.1; -; Genomic_DNA.
DR PIR; E69892; E69892.
DR RefSeq; NP_389697.1; NC_000964.3.
DR RefSeq; WP_003231534.1; NZ_JNCM01000035.1.
DR PDB; 3GTN; X-ray; 2.68 A; A/B=33-422.
DR PDB; 3KL0; X-ray; 1.64 A; A/B/C/D=33-422.
DR PDB; 3KL3; X-ray; 2.33 A; A/B/C/D=33-422.
DR PDB; 3KL5; X-ray; 2.59 A; A/B/C/D=33-422.
DR PDBsum; 3GTN; -.
DR PDBsum; 3KL0; -.
DR PDBsum; 3KL3; -.
DR PDBsum; 3KL5; -.
DR AlphaFoldDB; Q45070; -.
DR SMR; Q45070; -.
DR STRING; 224308.BSU18150; -.
DR CAZy; GH30; Glycoside Hydrolase Family 30.
DR PaxDb; Q45070; -.
DR PRIDE; Q45070; -.
DR EnsemblBacteria; CAB13698; CAB13698; BSU_18150.
DR GeneID; 937052; -.
DR KEGG; bsu:BSU18150; -.
DR PATRIC; fig|224308.179.peg.1979; -.
DR eggNOG; COG5520; Bacteria.
DR InParanoid; Q45070; -.
DR OMA; YDKYAAY; -.
DR PhylomeDB; Q45070; -.
DR BioCyc; BSUB:BSU18150-MON; -.
DR BioCyc; MetaCyc:BSU18150-MON; -.
DR BRENDA; 3.2.1.136; 658.
DR SABIO-RK; Q45070; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; Q45070; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR GO; GO:0033940; F:glucuronoarabinoxylan endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; PTHR11069; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..422
FT /note="Glucuronoxylanase XynC"
FT /id="PRO_0000278646"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:21256135"
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:21256135"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3KL5"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3KL0"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 379..388
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:3KL0"
FT STRAND 412..422
FT /evidence="ECO:0007829|PDB:3KL0"
SQ SEQUENCE 422 AA; 47337 MW; FEEB750E3B9DAAB8 CRC64;
MIPRIKKTIC VLLVCFTMLS VMLGPGATEV LAASDVTVNV SAEKQVIRGF GGMNHPAWAG
DLTAAQRETA FGNGQNQLGF SILRIHVDEN RNNWYKEVET AKSAVKHGAI VFASPWNPPS
DMVETFNRNG DTSAKRLKYN KYAAYAQHLN DFVTFMKNNG VNLYAISVQN EPDYAHEWTW
WTPQEILRFM RENAGSINAR VIAPESFQYL KNLSDPILND PQALANMDIL GTHLYGTQVS
QFPYPLFKQK GAGKDLWMTE VYYPNSDTNS ADRWPEALDV SQHIHNAMVE GDFQAYVWWY
IRRSYGPMKE DGTISKRGYN MAHFSKFVRP GYVRIDATKN PNANVYVSAY KGDNKVVIVA
INKSNTGVNQ NFVLQNGSAS NVSRWITSSS SNLQPGTNLT VSGNHFWAHL PAQSVTTFVV
NR
