ID A0A066ZBI8_9ACTN Unreviewed; 490 AA.
AC A0A066ZBI8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=KCH_07360 {ECO:0000313|EMBL:KDN87520.1};
OS Kitasatospora cheerisanensis KCTC 2395.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN87520.1, ECO:0000313|Proteomes:UP000027178};
RN [1] {ECO:0000313|EMBL:KDN87520.1, ECO:0000313|Proteomes:UP000027178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN87520.1,
RC ECO:0000313|Proteomes:UP000027178};
RA Nam D.H.;
RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
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|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:KDN87520.1}.
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DR EMBL; JNBY01000033; KDN87520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066ZBI8; -.
DR PATRIC; fig|1348663.4.peg.702; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_3_0_11; -.
DR OrthoDB; 4241492at2; -.
DR Proteomes; UP000027178; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 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:UP000027178};
KW Xylan degradation {ECO:0000313|EMBL:KDN87520.1}.
FT DOMAIN 34..335
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 490 AA; 52159 MW; 63ED92C35163AC58 CRC64;
MAQREDPPPH GRCSGRLRGA RPGRRPRRRP AAQAAGASTL GAAAAGSNRY FGTAVPTGKL
GDSTYATVLD REFNMITPEN EMKWDTVEPS RGSFNFGPAD SIVNHAAAHG QRMRGHTLVW
HSQLPSWVSS IGDANTLRSV MNNHITQEMT HYKGKIYAWD VVNEAFADNG SGQHRSSVFQ
NLLGNGFIEE AFRTARSVDP SAKLCYNDYS IENWSDAKTQ GVYSMVKDFK SRGVPIDCVG
FQSHFGSGGA PSSFRTTLSN FAALGVDVQI TELDIAQASA TAYGDAVQSC LDVARCTGIT
VWGIRDSDSW RTGENPLLFD NSGNKKAAYG TVLNALNNSG GGGTPSGGIV SGTVYTLTDV
AAGRVLDEPS GQTGNGTQLQ VWDANGSAAN QQWRATQNSD GSYTLVNIAS GRALDEPGGQ
TGNGTRMQVW DSNGGANQHW RATRNGDGSY TLLNAASGRA LEIPGGQTGN GSPVQIWDSN
GGANQHWNFK
//