ID A0A0H2KZS8_9MICO Unreviewed; 1282 AA.
AC A0A0H2KZS8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=FB00_17525 {ECO:0000313|EMBL:KLN33452.1};
OS Cellulosimicrobium funkei.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN33452.1, ECO:0000313|Proteomes:UP000035265};
RN [1] {ECO:0000313|EMBL:KLN33452.1, ECO:0000313|Proteomes:UP000035265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U11 {ECO:0000313|EMBL:KLN33452.1,
RC ECO:0000313|Proteomes:UP000035265};
RA Hu C., Gong Y., Wan W., Jiang M.;
RT "Cellulosimicrobium funkei U11 genome.";
RL Submitted (MAY-2014) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLN33452.1}.
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DR EMBL; JNBQ01000034; KLN33452.1; -; Genomic_DNA.
DR STRING; 264251.FB00_17525; -.
DR PATRIC; fig|264251.5.peg.3555; -.
DR Proteomes; UP000035265; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00005; CBM9_like_1; 1.
DR CDD; cd10917; CE4_NodB_like_6s_7s; 1.
DR Gene3D; 2.60.40.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF06452; CBM9_1; 1.
DR Pfam; PF02018; CBM_4_9; 2.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49344; CBD9-like; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000035265}.
FT DOMAIN 141..325
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 492..835
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 1282 AA; 134095 MW; 05556B774704A99F CRC64;
MTGRTADWHG VATDALALLQ PGVAYEVEAW VKLPAGTTGS SGVHFTVQET GASGTAYTWV
GGAVATTADG WVEIGGTYTL PAGLTSASLY VEAAPVAGAH PSFLLDDVRV ATVATDPGDV
VPGGAVNPVP TPVRLAEGTG DVAALTFDDG PNPGTTPALL DFLAEHDLHA VFCVIGQNVQ
APGGAELLRR IVDEGHVLCN HSTGYADMGA WSADQVRADL VENLGILRDA LGDPEYPVPF
FRAPNGSWGA TPEVAVALGM QPLAVVNTIS DWETQDVETL TANLRAAMRP GEVVLAHDGG
GDRAGTLAAV ETVVAERLAA GWEFTFPVGT PPRGGEVLLE TGFEDGLGGW VPRAGDATTP
SLDLTDVAHG GAQAAVVSGR DGQGDGIGHD VTGLLAVGTT YELSAWVRFA EGQPADDVWL
SIARTVDGAT SYSTLAQLAG ITSTGWTQIT ATFPGAAADE ALLYLETDYN GDNTSDLLVD
DVVLRVPPPP AVEDLTGIKE TVDVPVGVAI DSRETSGAAS ELLLRHFDQV TAENHMKPEA
WYDEDRTFRT HPEATALMDY AAAHDLRVYG HVLVWHSQTP AWFFEGADGA PLTTSEADRQ
VLRDRLRTHV FSVAQALADA YGPFGGDNPL TAFDVVNEVV SDGAENPDGL RRSEWFRILG
EEYLDLAFAY ADEAFNDVYA DPAATERGER PVALFINDYN TEQGGKQDRY HALVERLLAR
GVPVDGVGHQ FHVSLAMPVS ALDGAIERFA DLPVTQAVTE LDVTTGTPVT QASLVEQGYY
YRDAFRVFRA HADDLYSVTV WGLTDGRSWR VDSGAPLVFD DALKAKPAYH GVVDGELPAR
LRTADVFAGD VPLDGDATAS PDWQRLPLHT FAAPGGGAGG EVGFQLRWSP DHLTAFASVD
DATDDAADAV TFALDGTEHA VGRDGTTSAG VSAEVTERAG GYDVVAHLPL DAATAGDTLA
LDVRVTDAGT DGGAISAWNT PGATGTLRLL EELSYLEVAH ASAAPAVDGE VDAVWAEAGA
PVTTAKEVQG SGGAVATVRT LWRDRTLYVL AEVADPVVDV SGSDPWVQDS VEVYVDAGNA
KNGAYRDLDT QIRVSAENAV SFGTGDEAAQ RARVTSATTR TADGYVVELA VDLSDQGGEG
TFHGLDLQVN DASDGARTAI RNWADPSGAG YQSTARWGVA RLVGADAAPE VALDVEASAR
CLAGKAYVAV RATNREDVPV DVTLTTPYGS RTFTAVAPGA NAYQSFAVRA TSVPAGTATV
SAVLDGGRVT STRDVAVEAR TC
//
