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Database: UniProt
Entry: C4RGY4_MICS3
LinkDB: C4RGY4_MICS3
Original site: C4RGY4_MICS3 
ID   C4RGY4_MICS3            Unreviewed;       442 AA.
AC   C4RGY4;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=MCAG_00660 {ECO:0000313|EMBL:EEP70333.1};
OS   Micromonospora sp. (strain ATCC 39149 / NRRL 15099 / SCC 1413).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=219305 {ECO:0000313|EMBL:EEP70333.1, ECO:0000313|Proteomes:UP000010307};
RN   [1] {ECO:0000313|Proteomes:UP000010307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39149 / NRRL 15099 / SCC 1413
RC   {ECO:0000313|Proteomes:UP000010307};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., 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   Galagan J., Nusbaum C., Birren B.;
RT   "The genome sequence of Micromonospora carbonacea var. africana strain ATCC
RT   39149.";
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; GG657738; EEP70333.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4RGY4; -.
DR   STRING; 219305.MCAG_00660; -.
DR   eggNOG; COG3693; Bacteria.
DR   HOGENOM; CLU_020161_3_0_11; -.
DR   OMA; YSWRASG; -.
DR   Proteomes; UP000010307; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51173; CBM2; 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:UP000010307};
KW   Xylan degradation {ECO:0000313|EMBL:EEP70333.1}.
FT   DOMAIN          9..308
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          342..442
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          312..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..346
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        243
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   442 AA;  46178 MW;  CE597A67FD792E8B CRC64;
     MTVALAPAAS AGTTLRAASA EKGRYFGAAV ATGKLSNSTY TTVLNREFNS VVAENEMKWD
     ATEPQPGQFN YSGGDRLVNH ARANGMSVRG HALLWHQQQP GWAQNMSGSA LRSAMINHVT
     QVATHFRGQI YAWDVVNEAF ADGGSGARRD SNLQRTGNDW IEAAFRAARA ADPGAKLCYN
     DYNTDGINAK STGIYNMVRD FKSRGVPIDC VGFQSHLGTS LASDYQANLQ RFADLGVEVQ
     ITELDVMTGS NQANIFGAVT RACMNVSRCT GITVWGVRDC DSWRGSDNAL LFDCNGNKKP
     AYDAVLNALN AGGGIPNPTT PPPNPTTPPP NPTTPPPNPT TPPPGPGGCS ASVSANSWPG
     GFVVAVKVTA GSSGTRGWNV SVTLPGGSSV TGTWSATASG STGTVRFANV DYNGQLAAGQ
     VTEFGFQGNG TAPTQTPTCT AS
//
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