UniProt: S4MGR3

Database: UniProt
Entry: S4MGR3_9ACTN

LinkDB:  S4MGR3_9ACTN 
Original site:  S4MGR3_9ACTN

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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 (10)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (3)   
All databases (15)   

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ID   S4MGR3_9ACTN            Unreviewed;       224 AA.
AC   S4MGR3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=STAFG_8182 {ECO:0000313|EMBL:EPJ34755.1};
OS   Streptomyces afghaniensis 772.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ34755.1, ECO:0000313|Proteomes:UP000015001};
RN   [1] {ECO:0000313|EMBL:EPJ34755.1, ECO:0000313|Proteomes:UP000015001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=772 {ECO:0000313|EMBL:EPJ34755.1,
RC   ECO:0000313|Proteomes:UP000015001};
RA   Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA   Goodfellow M., Mueller M.;
RT   "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT   Compounds of the Julimycin B-Complex.";
RL   Submitted (FEB-2013) 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, ECO:0000256|RuleBase:RU362015};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097,
CC       ECO:0000256|RuleBase:RU362015}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPJ34755.1}.
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DR   EMBL; AOPY01001682; EPJ34755.1; -; Genomic_DNA.
DR   RefSeq; WP_020277009.1; NZ_KE354460.1.
DR   AlphaFoldDB; S4MGR3; -.
DR   PATRIC; fig|1283301.3.peg.8121; -.
DR   HOGENOM; CLU_052631_0_0_11; -.
DR   OrthoDB; 9763050at2; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000015001; 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   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; 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:UP000015001};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..224
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004521350"
FT   DOMAIN          37..224
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   224 AA;  24552 MW;  C0A16CF054E5192D CRC64;
     MKKSSSRLRL LISSVCTMLL VAFATIAMPG TAHADTVVTS NKTGTDNGYF YSFWTDAPGT
     VSMTLSSGGK YSTSWRNTGN FVAGKGWSNG ARRTVNYSGT FNPSGNAYLT LYGWTANPLV
     EYYIVDNWGT YRPTGQYKGT VTSDGGTYDI YKTTRYNAPS VEGVRTFDQY WSVRQSKRTG
     GTITAGNHFD AWARAGMPMG NFKYYMIMAT EGYQSSGSSS ITVR
//

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