ID A0A0K2AZT5_STRA7 Unreviewed; 474 AA.
AC A0A0K2AZT5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN Name=xlnA {ECO:0000313|EMBL:AKZ58635.1};
GN ORFNames=SAM23877_5590 {ECO:0000313|EMBL:AKZ58635.1};
OS Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 /
OS NBRC 12836 / NRRL B-2516).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=278992 {ECO:0000313|EMBL:AKZ58635.1, ECO:0000313|Proteomes:UP000061018};
RN [1] {ECO:0000313|Proteomes:UP000061018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL
RC B-2516 {ECO:0000313|Proteomes:UP000061018};
RX PubMed=26410452; DOI=10.1016/j.jbiotec.2015.09.020;
RA Thibessard A., Haas D., Gerbaud C., Aigle B., Lautru S., Pernodet J.L.,
RA Leblond P.;
RT "Complete genome sequence of Streptomyces ambofaciens ATCC 23877, the
RT spiramycin producer.";
RL J. Biotechnol. 214:117-118(2015).
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; CP012382; AKZ58635.1; -; Genomic_DNA.
DR RefSeq; WP_053138377.1; NZ_CP012382.1.
DR AlphaFoldDB; A0A0K2AZT5; -.
DR STRING; 1889.SAM40697_5079; -.
DR KEGG; samb:SAM23877_5590; -.
DR Proteomes; UP000061018; Chromosome.
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; -; 1.
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|ARBA:ARBA00023277,
KW 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|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000061018};
KW Xylan degradation {ECO:0000313|EMBL:AKZ58635.1}.
FT DOMAIN 40..340
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 474 AA; 50977 MW; 14CEB535771FB5FA CRC64;
MGSYALPRPV NRRKIRGLLL AVLVGILGAV TALVAPPTAH AAESTLGAAA AQSGRYFGTA
IASGKLGDST YTTIANREFN SVTAENEMKI DATEPQRGQF NFAAADRVYN WAVQNGKQVR
GHTLAWHSQQ PGWMQSLSGS ALREAMIGHI NGVMAHYKGK ITQWDVVNEA FADGSSGSRR
DSNLQRSGND WIEVAFRTAR AADPAAKLCY NDYNVEDWTW AKTQAMYAMV RDFKQRGVPI
DCVGFQSHFN SGSPYNSNFR TTLQNFAALG VDVAITELDI QGAPASTYTN VTNDCLAVPR
CLGITVWGVR DTDSWRSEQT PLLFNGDGSK KPAYTAVLNA LNGGSTTPPA DAGQIKGVGS
GRCLDVPSTT DGTQLRLWDC NSGTNQQWTY TDAGELRIQG NKCLDAAGTG NGVKVQVYSC
WGGDNQKWRL NSDGSIVGVQ SGRCLDAVAT GTANGTLIQL YTCSNGSNQR WTRT
//
