ID A0A239ICQ2_9ACTN Unreviewed; 445 AA.
AC A0A239ICQ2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN06264365_12852 {ECO:0000313|EMBL:SNS91325.1};
OS Actinoplanes regularis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=52697 {ECO:0000313|EMBL:SNS91325.1, ECO:0000313|Proteomes:UP000198415};
RN [1] {ECO:0000313|EMBL:SNS91325.1, ECO:0000313|Proteomes:UP000198415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43151 {ECO:0000313|EMBL:SNS91325.1,
RC ECO:0000313|Proteomes:UP000198415};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNR01000028; SNS91325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239ICQ2; -.
DR OrthoDB; 3255194at2; -.
DR Proteomes; UP000198415; 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:UP000198415};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:SNS91325.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..445
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039691466"
FT DOMAIN 31..330
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 345..445
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 445 AA; 45747 MW; 54B3606B416A7CF0 CRC64;
MPLFRKSRSL LLASAAAGIV VAAGVAVTGT AEAASTLGAS AAQSGRYFGA AIAAGKLGDG
TYTGILTREF NAVTPENEMK WDATEPSQGR FTFTNGDRIL NQGLSNGSKV RGHALLWHAQ
QPGWAQSLSG SALRTAAINH VTQVATHYKG KIYAWDVVNE AFADGGSGGR RDSNLQRTGN
DWIEAAFRAA RAADPNAKLC YNDYNTDGVN AKSTGIYNMV RDFKSRGVPI DCVGFQSHLG
TGIPGDYQAN LQRFADLGVD VQITELDVAQ GGNQAGVYAS VTRACMAVSR CTGITVWGIR
DSDSWRTGEN PLLFDNSGNK KAAYTSVLNA LNAGGTTPSS STSAPPQSGG ACGASVSLNS
WNGGFVATVR VIAGSAPING WTVTVTLPSG SAVTSAWSAT NTGTTGTVSF RNVAYNGQLA
AGGATEFGFQ GTGAGPTATP ACSAG
//