UniProt: A0A1M5H4M6

Database: UniProt
Entry: A0A1M5H4M6_9ALTE

LinkDB:  A0A1M5H4M6_9ALTE 
Original site:  A0A1M5H4M6_9ALTE

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (3)   
All databases (17)   

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ID   A0A1M5H4M6_9ALTE        Unreviewed;       491 AA.
AC   A0A1M5H4M6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
DE            EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
GN   ORFNames=SAMN05216361_1311 {ECO:0000313|EMBL:SHG10991.1};
OS   Marisediminitalea aggregata.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marisediminitalea.
OX   NCBI_TaxID=634436 {ECO:0000313|EMBL:SHG10991.1, ECO:0000313|Proteomes:UP000184520};
RN   [1] {ECO:0000313|Proteomes:UP000184520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.8995 {ECO:0000313|Proteomes:UP000184520};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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|PROSITE-ProRule:PRU01097};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097}.
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DR   EMBL; FQWD01000002; SHG10991.1; -; Genomic_DNA.
DR   RefSeq; WP_073319678.1; NZ_JANDJN010000031.1.
DR   AlphaFoldDB; A0A1M5H4M6; -.
DR   STRING; 634436.SAMN05216361_1311; -.
DR   OrthoDB; 9763050at2; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000184520; Unassembled WGS sequence.
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   Gene3D; 2.60.60.40; -; 2.
DR   InterPro; IPR031768; CBM60_xylan-bd.
DR   InterPro; IPR013320; ConA-like_dom_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   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF16841; CBM60; 2.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01097};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01097};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184520};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..491
FT                   /note="endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013290960"
FT   DOMAIN          25..221
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   REGION          215..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   491 AA;  51721 MW;  990FA86199DFFF70 CRC64;
     MGTKSKRLAM GLSLLTCSLG VTAQTLYENE TGTHDGFYYS FWKDSGNANF TLQPGGRYQS
     QWNSGTNNWV GGKGWNPGGR KTVNYSGYYG VDSSQNSYLA LYGWSQNPLV EYYIIESYGS
     YDPSSCAGGV DYGTFQSDGA TYKIRRCQRV QQPSIEGTQT FYQYFSVRQP IKGYGNISGT
     ITTGNHFDAW ASVGLNLGTF NYMVMATEGY QSSGSSDITV SEGSANSGGG NSGGGSTGGT
     GSPSSTDIVV NARGVTGTEH INLLIDGNVV ADWTLTTTTS SYVYSGNAAG DVQVEYDNDT
     SGADVILDSV YVNGETREAE SMEYNTATYG NGECGGGSYS ETMHCNGVIG FGGTGACFSG
     NCASASPGGN SGNDTITVRA QGVTGSEHIN LVIDGNVVAD WTLSSTMADY TYSGSASGNL
     QVQYDNDASG RDVVVDYVFV NGEIREAEDM EYNTANYANG QCGGGSYAET MHCNGVIGFG
     DTNACFSNSC N
//

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