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Database: UniProt
Entry: F7PGE0_9EURY
LinkDB: F7PGE0_9EURY
Original site: F7PGE0_9EURY 
ID   F7PGE0_9EURY            Unreviewed;       520 AA.
AC   F7PGE0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590};
DE            EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590};
GN   ORFNames=HLRTI_003068 {ECO:0000313|EMBL:ERJ04950.1}, HTIA_1703
GN   {ECO:0000313|EMBL:CCQ33829.1};
OS   Halorhabdus tiamatea SARL4B.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorhabdus.
OX   NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ04950.1, ECO:0000313|Proteomes:UP000003861};
RN   [1] {ECO:0000313|EMBL:ERJ04950.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ04950.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=21705593; DOI=10.1128/JB.05462-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT   a deep-sea anoxic brine lake.";
RL   J. Bacteriol. 193:4553-4554(2011).
RN   [2] {ECO:0000313|EMBL:ERJ04950.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ04950.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT   the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(2013).
RN   [3] {ECO:0000313|EMBL:CCQ33829.1, ECO:0000313|Proteomes:UP000015381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC   SARL4B {ECO:0000313|EMBL:CCQ33829.1};
RX   PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA   Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA   Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA   Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA   Golyshin P.N., Teeling H.;
RT   "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT   identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT   lake as potential polysaccharide degrader.";
RL   Environ. Microbiol. 16:2525-2537(2014).
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   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
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DR   EMBL; HF571520; CCQ33829.1; -; Genomic_DNA.
DR   EMBL; AFNT02000049; ERJ04950.1; -; Genomic_DNA.
DR   RefSeq; WP_008524290.1; NZ_AFNT02000049.1.
DR   STRING; 1033806.HTIA_1703; -.
DR   GeneID; 23799744; -.
DR   KEGG; hti:HTIA_1703; -.
DR   PATRIC; fig|1033806.12.peg.1693; -.
DR   eggNOG; arCOG09007; Archaea.
DR   HOGENOM; CLU_519371_0_0_2; -.
DR   OrthoDB; 8638at2157; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000003861; Unassembled WGS sequence.
DR   Proteomes; UP000015381; Chromosome.
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; cd04080; CBM6_cellulase-like; 1.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00606; CBD_IV; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PROSITE; PS50093; PKD; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ERJ04950.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ERJ04950.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW   ECO:0000313|EMBL:CCQ33829.1}.
FT   DOMAIN          51..237
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   DOMAIN          274..415
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          438..520
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   REGION          228..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  54761 MW;  1C85CE9C23C2EB43 CRC64;
     MRKHDSDRNP DAESSENDLF GQFDRRSYLK GAAATVATGL GVGSLASPAA AITENQTGTH
     DGYFYSFWTN DQGSVEMTLE SGGSYSVDWS NTGNFVCGKG WETGARRDIE YTADYNPQGN
     SYLCLYGWTT DPLVEYYIIE DYGSYKPGDS YQGTHTTDGS TYEIYTSERV EKPSIEGTAT
     FTQYWSIRQN SRTSGTITTG NHFDAWESVG LNMGSHDYQI LATEGYQSSG SASVTIGESG
     GGGDTGGGGD DGGDTGGDTG SQQPYNGTPH AVPGRIQAEE YDQGGSGVAY SDNTAENEGG
     AMRTGEGVDI SSNSAGSGYS IGYIESGEWV EYTVDVQQSG DYTLDALVAS DSGGGSFHLE
     VNGQNVSGDL SFGATGGWDS WETVSTSGVS LDAGQQVIRV SMDESWWDLN YLDLSLDGNG
     GDDGGDTGGD DGNDTGSLVA EIDPNTTSAS VGDLVQFNIT DTTGPGSYIT SLEWDLGNGV
     TGTGWYIDER YQSAGSYTVS LTATDNEGTS TTDEVTVTIS
//
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