ID H5XHV5_9PSEU Unreviewed; 460 AA.
AC H5XHV5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SaccyDRAFT_0633 {ECO:0000313|EMBL:EHR59561.1};
OS Saccharomonospora cyanea NA-134.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882082 {ECO:0000313|EMBL:EHR59561.1};
RN [1] {ECO:0000313|EMBL:EHR59561.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA-134 {ECO:0000313|EMBL:EHR59561.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA Klenk H.-P., Woyke T.;
RT "The Noncontiguous Finished sequence of Saccharomonospora cyanea NA-134.";
RL Submitted (NOV-2011) 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; CM001440; EHR59561.1; -; Genomic_DNA.
DR RefSeq; WP_005453499.1; NZ_CM001440.1.
DR AlphaFoldDB; H5XHV5; -.
DR STRING; 882082.SaccyDRAFT_0633; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_3_0_11; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000002791; Chromosome.
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|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 Xylan degradation {ECO:0000313|EMBL:EHR59561.1}.
FT DOMAIN 42..347
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 357..460
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 281
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 460 AA; 49290 MW; F98D059A3AA53597 CRC64;
MSTAHQRRFG PRRIGVRIRK AVAAAAVGAV TAGGFVAAAG TASAQTTLGD AAAAQGRYFG
VAVAAGRLGE PDYTATLNRE FNSVTAENSW KWESLQPSPG YFDFSTADRI AEHARQQGME
LRGHTLVWHS QLPGWVENIG SADELRAVMN NHITTVMEHY KGQVRSWDVV NEAFADGGSG
ARRDSVFQRL LGDGWIEEAF RTARAADPDA TLCYNDYNTD AWNTAKTQAV YNMVADFVSR
GVPIDCVGFQ AHFNSGNPVP ENYHVTLQNF ADLGVEVQIT ELDIAGWGDS QAQQYAGVTL
ACLAVPQCSG ITVWGVTDKY SWRAEDTPLL FDGDYNPKQA YHAVLETLGG SGGGGGGGDD
GAACTVTYDE TQRWGDRFNG RVTVRAGDEA ISSWSTTVTV HPPQKITATW NGEASWDYSG
DVMTMRSYSG LPAGGETSFG FTVMANGNWA APTLGSCTAS
//
