ID D9T5J8_MICAI Unreviewed; 536 AA.
AC D9T5J8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN OrderedLocusNames=Micau_0285 {ECO:0000313|EMBL:ADL43853.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL43853.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL43853.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) 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}.
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DR EMBL; CP002162; ADL43853.1; -; Genomic_DNA.
DR AlphaFoldDB; D9T5J8; -.
DR STRING; 644283.Micau_0285; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR KEGG; mau:Micau_0285; -.
DR eggNOG; COG2226; Bacteria.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_507892_0_0_11; -.
DR OrthoDB; 3255194at2; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF08241; Methyltransf_11; 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 SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 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:UP000001908}.
FT DOMAIN 203..376
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 381..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 58123 MW; E7985A997A633BCA CRC64;
MVNTTRNLGL GHGSAFGERG VAKRLGTLSR HTSLTGRRLL EIGCGDGTYT MRLVGAFEQI
EAVDIQQDRL ALFRERLADY PAAAQKINVR ELSATELDYP DESFDLVTAI EVVEHIDDLD
AALRQVRRVL VPGGCFALTT PNRWFPFETH GFLIRGKRYR PARGPFLPWI VPLHRRLADA
RCFTARGLSA QLRRAGLEPV AVDYVNEAFN EDGSRRQSNL QGTGNDWIEV AFRTARAADP
SVKLCYNDYN IENWSYGKTQ GVYNMIRDFK SRGVPIDCVG LQTHFTGGSS LPGNFQTTLS
SFAALGVDVA LTEVDVTNSS TSQYAGLTQA CLNVPRCIGI TVWGVRDSDS WRSNENPLLF
DGGGNKKAAY TSVLNVLNAA TPNPTPTGTA SPTAGPTPTA GPTTPPPTNG ASRIVGNQSG
RCIDVPNSSQ SNGTRVQLYD CHGLTNQRWT YTSSRQLTVY GSMCLDAAGS GNGSAVQIYS
CNGQTNQQWN VNSNGTITGV QSGRCLDVWG TGNGQQVQIY DCNGQANQRF QLVATS
//
