ID A0A0D0X5W1_9ACTN Unreviewed; 958 AA.
AC A0A0D0X5W1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=1,4-beta-xylanase {ECO:0000313|EMBL:KIR64890.1};
GN ORFNames=TK50_04755 {ECO:0000313|EMBL:KIR64890.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR64890.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR64890.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR64890.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KIR64890.1}.
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DR EMBL; JXSX01000001; KIR64890.1; -; Genomic_DNA.
DR RefSeq; WP_043961640.1; NZ_JXSX01000001.1.
DR AlphaFoldDB; A0A0D0X5W1; -.
DR PATRIC; fig|47853.6.peg.1012; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000032254; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd09001; GH43_FsAxh1-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000313|EMBL:KIR64890.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KIR64890.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIR64890.1};
KW Polysaccharide degradation {ECO:0000313|EMBL:KIR64890.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032254};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:KIR64890.1}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..958
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002240782"
FT DOMAIN 396..524
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 563..777
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT REGION 21..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 169
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 958 AA; 102517 MW; AD83BFD43C376B9E CRC64;
MGALLLCAGV VTIGTAAQAA DEWSPESSHT STDRGDGTYT VPLLRSDVPD ISVERVPAAE
NDEGRDIYYM ISTTMHLSPG APIMKSYDLV NWETVNYVFD RASIGDSFSL RNGQNSYGQG
QWASSLRYHD GMYYVAFNTN NLNGAYIYRT DDIENGAWQR TALGRGLHDP SLFFDVDGTP
YIFYGSGGTS AVRLNAGLTA IEQDYPNIFT AADYAGQPFI GGLFEGAQFY HIDGWYYAVI
ITWPSGQGRQ VVMFRSKDLL GRYTSAGGVN TYEARGVLNS NGFAQGSLVP VARAGGGTDW
HGMFFRDTFP IGRIPALIPA TWSGGWPTFG NNGVVPVDGA FAKPIRLSPA EEALERQKSI
VASDDFANDA PHKAYQDEEW TIPTPPDLDE SLLGVELLGN AGFEAGSVSP WAAQFGATLA
LEPADAASGS AALRVGNRTL NGSGPNQNLA GKLQHGVTYT VSAKIKYTSG PASVRFNLAA
DWGSGVQVMT FGTVPVGQWT TVTGQYTFPA TANLANVKFA VETPWGNPQP ASSTVEYLID
DVSVVGQPVT TEHPTEAEIA PNGSRLDLAW EWNHAPDNRY WSLTDREGWL RLTTGKVVTG
QYVYTKLSNR AELAWFEEAR NTLSQRTFGP RQSAETRMDI SGMRNGDVAG LAAYNRGFSY
VAVKRVDGQN TLGVVNRGQP FAVDLDQAAL ESFLPGTTVP LGDATVVHVK ADLDFASPVG
QLWTTFYYSL DGLTWTQLGN RVGPQTLDGS LAHFMGHRVG LFNYATQATG GRVDFDHYLL
SDTLTAQGQP LDTGALDAAI AHAETLDSRH YPADAWTAMR AALASAKAAR AGRFGTQNQI
DAPQRSLSFQ LARLGVLRAE PELPVTASAQ ARCVGGRAYV AVQATNGHTA PVDITLETAY
GTRTVTGVAP GANAYQSFTT RATSIPAGTA TIRATGTIDG TTVTTVTTAN HPALSCGA
//
