(data stored in SCRATCH zone)

SWISSPROT: C7PX75_CATAD

ID   C7PX75_CATAD            Unreviewed;       494 AA.
AC   C7PX75;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   16-JAN-2019, entry version 67.
DE   RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|PROSITE-ProRule:PRU01097};
DE            EC=3.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU01097};
GN   OrderedLocusNames=Caci_0474 {ECO:0000313|EMBL:ACU69426.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69426.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69426.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU01097};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000256|PROSITE-ProRule:PRU01097}.
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DR   EMBL; CP001700; ACU69426.1; -; Genomic_DNA.
DR   STRING; 479433.Caci_0474; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   EnsemblBacteria; ACU69426; ACU69426; Caci_0474.
DR   KEGG; cai:Caci_0474; -.
DR   eggNOG; ENOG4107T94; Bacteria.
DR   eggNOG; ENOG410YH6C; LUCA.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR006644; Cadg.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR008009; He_PIG.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF05345; He_PIG; 2.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00736; CADG; 2.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49313; SSF49313; 2.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7PX75.
DR   SWISS-2DPAGE; C7PX75.
KW   Carbohydrate metabolism {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Glycosidase {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000313|EMBL:ACU69426.1};
KW   Polysaccharide degradation {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|PROSITE-ProRule:PRU01097}.
FT   SIGNAL        1     15       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        16    494       Endo-1,4-beta-xylanase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002980425.
FT   DOMAIN       18    204       GH11. {ECO:0000259|PROSITE:PS51761}.
FT   DOMAIN      386    494       CBM2. {ECO:0000259|PROSITE:PS51173}.
FT   ACT_SITE    102    102       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    191    191       Proton donor. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
SQ   SEQUENCE   494 AA;  49816 MW;  C275C2859EFDAEFA CRC64;
     MLAGVMALLP GTAGAATTIC SSQTNTVSGY WYSFWTEGSG SACMTFGSAG NYSTSWSNAG
     NFVAGLGWST GGRKTVSYSG SFNPSGNGYL SLYGWTTNPL VEYYITDSWG SYRPTGTYKG
     TVTSDGGTYD IYETTRYNEP SIIGTATFNQ YWAVRQSKRV GGTITTGNFF DAWASHGMNM
     GQYNYMILAT EGYQSSGNSN ITIGGSVTNT VTVTNPGSQS TTAGSPASVQ VHASDSASGQ
     TLAYTASGLP PGLSINSGSG LISGTPTTPG SYQVTVTGTD TTGAKGSATF TWTVGSETGT
     LVTVTSPGNQ TGSVGTAISP IQIQATDSAG QALTYSATGL PAGLSISSSG VISGTPTAAG
     TSDVTVTASD SSGSGSATFT WSISGGGTTT GVCHATYART SEWPGGFTAN VTIANTGTTA
     VNGWTLGWSF PGDQKITNAW SATATQSGSN VTATNVAYNG SIAPGGTTSF GFQGTYGSND
     SSPTAFTLNG TACS
//

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