ID I0L2H8_9ACTN Unreviewed; 605 AA.
AC I0L2H8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Extracellular endo-1,4-beta-xylanase {ECO:0000313|EMBL:CCH18025.1};
GN Name=xlnA {ECO:0000313|EMBL:CCH18025.1};
GN ORFNames=MILUP08_42956 {ECO:0000313|EMBL:CCH18025.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH18025.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:CCH18025.1}.
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DR EMBL; CAIE01000022; CCH18025.1; -; Genomic_DNA.
DR AlphaFoldDB; I0L2H8; -.
DR STRING; 1150864.MILUP08_42956; -.
DR eggNOG; COG3507; Bacteria.
DR eggNOG; COG3693; Bacteria.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000003448; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd18618; GH43_Xsa43E-like; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF6; -; 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:CCH18025.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CCH18025.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCH18025.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:CCH18025.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:CCH18025.1}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..605
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003630843"
FT DOMAIN 339..462
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 500..605
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 464..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 224
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 163
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 605 AA; 63905 MW; 27753C364AF04412 CRC64;
MHRTPPPRTK NRLRRGVAWL VSMLLISTLA PATAAHADNP IVQHIYTADP APLVHDGRVY
LYTGHDEDGS TYFTMKDWRV WSSADMVNWT DHGSPLSLNT FSWASANAWA GQVIARNGKF
YWYVPVTARA TNSMAIGVAV ADSPTGPFRD AIGRPLVGNG EIDPTVFIDD DGQAYLYWGN
PNLWYVRLNA DMISYSGSAT KIPLTTAGFG TRTGNASRPT LYEEGPWVYK RNGLYYNVFA
AECCSEFIGY STATGPTGPW TYRGTIMPRQ GASFTNHPGV IDFNGGSYFF YHNGALPGGS
GYTRSVAVEK FTYNTNGTIP TITMTTTGAP QIGTLNPYGR QEAETIAWGS GIETEPASEG
GMNVGFIENG DYIKVKGVGF GTGATSFSAR VASATSGGTV ELRLGSPTGT RVGSCAVPGT
GGWQTWQTVS CPVSGATGTQ DLYLRFTGGT GNLFNLNWWQ FQAGGTTTPT PTPTPTSTPT
PTPTPTPTPT PTSTPTPTPT VPAGQSCAVT NTVVNTWQGG FEGRLTVTNS GASALGGWRV
TFTLPSGQTV SQVWNGALTQ TGSQVTVTNA AYNGQLAPGT STTAGYLSTS ATSSPPTITP
TCSPA
//
