ID D9XAI6_STRVT Unreviewed; 678 AA.
AC D9XAI6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SSQG_00641 {ECO:0000313|EMBL:EFL30123.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL30123.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
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:0000256|ARBA:ARBA00001462};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|RuleBase:RU361174}.
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DR EMBL; GG657757; EFL30123.1; -; Genomic_DNA.
DR AlphaFoldDB; D9XAI6; -.
DR STRING; 591159.SSQG_00641; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_016688_0_0_11; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
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:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08987; GH62; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR40631:SF2; ALPHA-L-ARABINOFURANOSIDASE; 1.
DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000004184};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:EFL30123.1}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..678
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003132002"
FT DOMAIN 32..333
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 334..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 270
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 678 AA; 73807 MW; 6FB7271192C32583 CRC64;
MKHSGRRRAS LLALVATAAL VTPVAATAAP DAVRASTLGA QAAQSGRYFG TAVAAGRLGD
GTYTSILDRE FNSVTPENEM KWDTTEPSRG SFNFGPADQI ANRAQARGQR LRGHTLVWHS
QLPGWVSSIR DANTLRGVMN NHITTVMNRY KSRIHSWDVV NEAFADGGSG QMRSSVFRDV
LGTGFIEQAF RTARSADPAA KLCYNDYNIE NWSDAKTQGV YRMVRDFKSR GVPIDCVGLQ
SHFGAGGPPA SFQTTLSSFA ALGVDVQITE LDIAQASPTA YANTVRACMN VARCTGITVW
GIRDSDSWRS GENPLLFDRN GNKKPAYNSV LTTLGGTPTT RSTPAVTSGT PTGPRSATNT
AALPSRYSWS SSGPLISPKP DSTHNIAGIK DPTVVQYNGK YHVFASTASS SGYNLVYLNF
SDWSQAGSAT HHYLDRTAIG SGYRAAPQVF YYAPQRLWYL VYQTGNASYS TNPDISNPNG
WSAPRNFYSS MPDIIRQNIG NGYWVDMWVI CDSANCYLFS SDDNGHLYRS QTTVGQFPNG
FTNTVIAAQD SKYAMFEASN VYKVQGSNQY LLLVEAIGSD GRRYFRSWTS GSLAGSWAPL
ASSESNPFAR ASNVSFPSGA WTRDISHGEM IRAGYDQTLT IPACRLQYLY QGMNPNASGD
YNLLPWRLAL LTQTNSTC
//
