ID A4IP84_GEOTN Unreviewed; 333 AA.
AC A4IP84;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN Name=xynA2 {ECO:0000313|EMBL:ABO67138.1};
GN OrderedLocusNames=GTNG_1774 {ECO:0000313|EMBL:ABO67138.1};
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO67138.1, ECO:0000313|Proteomes:UP000001578};
RN [1] {ECO:0000313|EMBL:ABO67138.1, ECO:0000313|Proteomes:UP000001578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2 {ECO:0000313|EMBL:ABO67138.1,
RC ECO:0000313|Proteomes:UP000001578};
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681,
CC ECO:0000256|RuleBase:RU361174};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|RuleBase:RU361174}.
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DR EMBL; CP000557; ABO67138.1; -; Genomic_DNA.
DR AlphaFoldDB; A4IP84; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR KEGG; gtn:GTNG_1774; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_6_1_9; -.
DR Proteomes; UP000001578; 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 Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
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; 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.
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:ABO67138.1};
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:ABO67138.1}.
FT DOMAIN 4..333
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 333 AA; 39027 MW; 7DAA86F5537BBF05 CRC64;
MSVSQSLPSL REVFANDFRI GAAVNPVTIE SQKQLLISHV NSLTAENHMK FEHLQPEEGR
FTFDIADRIV DFARSHHMAV RGHTLVWHNQ TPDWVFQDGQ GHFISRDVLL ERMKSHISAV
VRRYKGKVYC WDVVNEAVAD EGSEWLRSSK WRQIIGDDFI EQAFLCAHEA DPDALLFYND
YNECFPKKRE KIYTLVKSLR DKGIPIHGIG MQAHWSLTRP SLDEIRAAIE RYASLDVVLH
ITELDVSMFE FHDHRKDLAA PTNEMIERQA ERYEQIFTLF KEYRDVIESV TFWGMADDYT
WLDHFPVQGR KNWPFLFDEQ HEPKSAFWRV ASI
//
