ID E8X6C6_GRATM Unreviewed; 376 AA.
AC E8X6C6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN OrderedLocusNames=AciX9_4234 {ECO:0000313|EMBL:ADW71010.1};
OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OG Plasmid pACIX901 {ECO:0000313|EMBL:ADW71010.1,
OG ECO:0000313|Proteomes:UP000000343}.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN [1] {ECO:0000313|Proteomes:UP000000343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RC PLASMID=Plasmid pACIX901 {ECO:0000313|Proteomes:UP000000343};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA Haggblom M.M., Woyke T.;
RT "Complete sequence of plasmid1 of Acidobacterium sp. MP5ACTX9.";
RL Submitted (JAN-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; CP002481; ADW71010.1; -; Genomic_DNA.
DR RefSeq; WP_013572922.1; NC_015057.1.
DR AlphaFoldDB; E8X6C6; -.
DR KEGG; acm:AciX9_4234; -.
DR HOGENOM; CLU_020161_7_0_0; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000000343; Plasmid pACIX901.
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 Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|RuleBase:RU361174, ECO:0000313|EMBL:ADW71010.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Plasmid {ECO:0000313|EMBL:ADW71010.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000000343};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:ADW71010.1}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..376
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003234237"
FT DOMAIN 46..365
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 376 AA; 41538 MW; 22715FA59E09B81F CRC64;
MKPQPNRRTF LQTASAGLLG SALPAPLLAL SDNKQPWTPL GRLAQEKNIS FGFALNYRLL
SGNQDYDALV SRECTIVTPE NAMKWEAVHP EPDRYTFTQA DAILDFAQQH AMKIRGHAFC
WHRALPAWVT HDVTKQNAEE VLRQHIATVA GRYKGKLHSW DVVNEAIQLK DNQPGGWRNS
FWFQQLGPAY LDIAFDAASQ ADPAAILTYN DYGLEYENHS DSAKRKAVLT MLHDLKKHGI
PVRALGMQSH LRAGTGESFG SDLPSFIKEV RDLGLEIFVT ELDVDDSHLT VPDLARDSAI
ADVYKRYLDL VLSTTAVSVV ITWGAWDIVK VTGAEATSGP SAQHPLLFAP GGLPKLDAAL
VAQSFRTAPL QHQVRG
//
