(data stored in SCRATCH zone)

SWISSPROT: C7PX63_CATAD

ID   C7PX63_CATAD            Unreviewed;       337 AA.
AC   C7PX63;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015};
DE            EC=3.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015};
GN   OrderedLocusNames=Caci_0462 {ECO:0000313|EMBL:ACU69414.1};
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:ACU69414.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69414.1, 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: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans. {ECO:0000256|RuleBase:RU362015}.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097,
CC       ECO:0000256|RuleBase:RU362015}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000256|PROSITE-ProRule:PRU01097,
CC       ECO:0000256|RuleBase:RU362015}.
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DR   EMBL; CP001700; ACU69414.1; -; Genomic_DNA.
DR   RefSeq; WP_012784709.1; NC_013131.1.
DR   STRING; 479433.Caci_0462; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   EnsemblBacteria; ACU69414; ACU69414; Caci_0462.
DR   KEGG; cai:Caci_0462; -.
DR   eggNOG; ENOG4107T94; Bacteria.
DR   eggNOG; ENOG410YH6C; LUCA.
DR   HOGENOM; HOG000179135; -.
DR   OMA; QNSWNAS; -.
DR   OrthoDB; POG091H0EC9; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR008965; Carb-bd_dom.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR013320; ConA-like_dom.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7PX63.
DR   SWISS-2DPAGE; C7PX63.
KW   Carbohydrate metabolism {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000256|RuleBase:RU362015};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Glycosidase {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000256|RuleBase:RU362015, ECO:0000313|EMBL:ACU69414.1};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000256|RuleBase:RU362015, ECO:0000313|EMBL:ACU69414.1};
KW   Polysaccharide degradation {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000256|RuleBase:RU362015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|PROSITE-ProRule:PRU01097,
KW   ECO:0000256|RuleBase:RU362015, ECO:0000313|EMBL:ACU69414.1}.
FT   SIGNAL        1     39       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        40    337       Endo-1,4-beta-xylanase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002981330.
FT   DOMAIN       42    230       GH11 (glycosyl hydrolase family 11).
FT                                {ECO:0000259|PROSITE:PS51761}.
FT   DOMAIN      245    337       CBM2 (carbohydrate binding type-2).
FT                                {ECO:0000259|PROSITE:PS51173}.
FT   ACT_SITE    127    127       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    217    217       Proton donor. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
SQ   SEQUENCE   337 AA;  34535 MW;  4745DE0B0999E623 CRC64;
     MPGNSRLPGA RRSRRLRMFI GVVLALFLGA MLPSVPASAA TSICSNQTGT NSGYYYQMWS
     SGQGSACISL NSGNSYSSTW SGIGDFVAGV GWNPGDKSTK SFTGSLNANG GTSLVSLYGW
     STSPLVEYYV MENYVGSPPT AGTYMGQVTS DGGTFNIYEH QQVNQPSIQG TATFEQYLAI
     RTSPVSSGTI TMSNYINAWS SHGMNLGTLN YQILATEAWG GGSGSSNVSV SSGGGGGGGG
     GGGGGGGGGG SCTATLSAGS QGSNWYNLNV AVTGSSNWTV TMNMASPAVV YNTWNVSATW
     PSQYVMVAKP NGSGNNFGVT ISPNGQWTWP SVSCSSS
//

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