ID A0A1I6R0U3_9BACI Unreviewed; 1276 AA.
AC A0A1I6R0U3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN05421668_1057 {ECO:0000313|EMBL:SFS58283.1};
OS Halolactibacillus miurensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halolactibacillus.
OX NCBI_TaxID=306541 {ECO:0000313|EMBL:SFS58283.1, ECO:0000313|Proteomes:UP000199139};
RN [1] {ECO:0000313|EMBL:SFS58283.1, ECO:0000313|Proteomes:UP000199139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17074 {ECO:0000313|EMBL:SFS58283.1,
RC ECO:0000313|Proteomes:UP000199139};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR EMBL; FPAI01000005; SFS58283.1; -; Genomic_DNA.
DR RefSeq; WP_062321586.1; NZ_FPAI01000005.1.
DR AlphaFoldDB; A0A1I6R0U3; -.
DR STRING; 306541.SAMN05421668_1057; -.
DR OrthoDB; 9809277at2; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000199139; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00005; CBM9_like_1; 1.
DR Gene3D; 2.60.40.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF06452; CBM9_1; 1.
DR Pfam; PF02018; CBM_4_9; 3.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Xylan degradation {ECO:0000313|EMBL:SFS58283.1}.
FT TRANSMEM 1247..1267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 519..855
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 1059..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 779
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 1276 AA; 142597 MW; 24BDB7749E10D47B CRC64;
MSKQKQSKWF IYFLITLMLL PNLSPLTVYA ETSDVILHHD FETDTDGWEA LDWGDSTSPL
TRELTETEAF SGQKSLEVSR EAYNSKLSFN LTDQLIEGES YKLSFSIKLK EGTETLRLAS
KHSYPGTTNE YPWVIGNNEV STEWVTFESE AIHYEPGTTE FIVYIESNQE VGTPAVYYLD
DIQMIQLEGE DTPEEPEGEA VSIIKHDFET ETHGWEKLSW SNEGLTTALT TDEAYTGDQS
LEVTRTGFGS KLSLNLTDQL TEGETYKLSF YLKLKEGTEQ LRLASKYSYP DTSNEYPWII
NTKEVGTEWV RFESGEINYM PGTTEFIVYL ESEQTEGTPS VYYLDDVEVV HLEKETTDDK
PAAEILSPID FESGEASGFV ARGEVEDLTV TDETNHTPDG SMSLKVENRS QNWHGPSLDV
YNYVDQGELY EVSAWVKMVE GSDELKLSTQ VGAGDTASYN NITSAQVTAN EWVNLKGTYR
YSSLGGGNLS IYVEGASATS SFYLDDVTFT KLETAPIVIE DITPIKDVYQ DDFLIGNAVS
MSEFEGIRLE LLKKHFNLVS AENAMKPSYA YDDEGNFDFN AEKLLVETAI EEGFDIHGHV
LVWHQQSRDA LYQDEEGNPL SREEALENMY THIETTMAAF KDYDDHLISW DVVNEAMLDS
ANAPYDDWES NLRQSGWYKA IGSDYIELAF KKARETADRL GLDVVLYYND YNDDQQNKAQ
SIYHMIKDIN ERYQEENPGE LLIQGMGMQS HYNMNTNPTN VRLSMERFIE LGVEIGVTEL
DVTAGSGGVQ TAKEANRQAY IYAELFSLYK EHAEHISRVT IWGLNDATSW RAEQSPLVFD
ANLQSKLAYE AIMDPETFLL NYEEEQVPVR EGQAIKTETT PILDGVEDGL YKEAMTLSVD
RFQQAWSTAT AEAKAVWDDD FLYVLVNVTN DVLDVTSANA WEQDSVEVFV DQLNSKAPNY
DAAEGIGQYR VNVENVQSFG NGNVYEGFKS ATKVNGTSYT VEMAIPLTNI TPSNETVIGF
DLQINDGEDG TRVGVATWND TSGQGFQDPS VFGEVTLVSD DTDETPTPGE PGEETPTPGE
PEEETPTPGD ENSTNNDTVI GLSKAPVRVS KGETIVIEDL KATIKMPNDL PEGTTITVGT
YDEETYTAAN GEKLNVRGEI ITVNLVFPEG FEGYEGEFKL TLGVNADADN PAVYYLGEDG
WELRGGDYDE ENGVIRLMVS GFSTYGVFET EVDDAAGETL PDTSTMMFNW SVIGAILLLV
SAGLFRVNKR KQTVKY
//
