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Database: UniProt
Entry: A0A0L8LKA6_9ACTN
LinkDB: A0A0L8LKA6_9ACTN
Original site: A0A0L8LKA6_9ACTN 
ID   A0A0L8LKA6_9ACTN        Unreviewed;      1737 AA.
AC   A0A0L8LKA6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Hydrolase {ECO:0000313|EMBL:KOG38567.1};
GN   ORFNames=ADK37_09590 {ECO:0000313|EMBL:KOG38567.1}, AQJ84_06190
GN   {ECO:0000313|EMBL:KUO00595.1};
OS   Streptomyces resistomycificus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=67356 {ECO:0000313|EMBL:KOG38567.1, ECO:0000313|Proteomes:UP000037251};
RN   [1] {ECO:0000313|EMBL:KOG38567.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL 2290 {ECO:0000313|EMBL:KOG38567.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000037251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2290 {ECO:0000313|Proteomes:UP000037251};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KUO00595.1, ECO:0000313|Proteomes:UP000052992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40133 {ECO:0000313|EMBL:KUO00595.1,
RC   ECO:0000313|Proteomes:UP000052992};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces resistomycificus DSM 40133, type
RT   strain for the species Streptomyces resistomycificus.";
RL   Submitted (OCT-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:KOG38567.1}.
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DR   EMBL; LGUS01000083; KOG38567.1; -; Genomic_DNA.
DR   EMBL; LMWZ01000003; KUO00595.1; -; Genomic_DNA.
DR   RefSeq; WP_053190767.1; NZ_LGUS01000083.1.
DR   STRING; 67356.AQJ84_06190; -.
DR   PATRIC; fig|67356.5.peg.2079; -.
DR   eggNOG; COG3507; Bacteria.
DR   eggNOG; COG5492; Bacteria.
DR   OrthoDB; 9758923at2; -.
DR   Proteomes; UP000037251; Unassembled WGS sequence.
DR   Proteomes; UP000052992; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08983; GH43_Bt3655-like; 1.
DR   CDD; cd09004; GH43_bXyl-like; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 2.60.40.2340; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR046780; aBig_2.
DR   InterPro; IPR011081; Big_4.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006558; LamG-like.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF20578; aBig_2; 2.
DR   Pfam; PF07532; Big_4; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 2.
DR   Pfam; PF13385; Laminin_G_3; 2.
DR   Pfam; PF18911; PKD_4; 1.
DR   SMART; SM00560; LamGL; 2.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49299; PKD domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KOG38567.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037251};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..1737
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011859012"
FT   DOMAIN          110..252
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   DOMAIN          909..1051
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   REGION          292..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        1314
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            1267
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   1737 AA;  184045 MW;  3B7976AB7CA2AC52 CRC64;
     MTYRARLRGR ARRLTGRLAG LTAASLLLGL GPAVPAQAAE TADTAEITDG LALWYPLDAA
     SGTAATDASG NGRTGTVNGT AGWSASGQGL AFNGSDTYIK VPDDVMKGMN AISVSMDVLI
     DSAQTTPYFI YGFGNTSAGN GNGYLFTTGN SLRTSIATGN WSTEQTTKPG DSHNLARAAW
     KHLTYTQTGT TGVLYEDGVE VGRNTAVTTT PGAIGSGTTT ANYIGKSVYS GDKLFKGRIR
     DFRVYDRALA DTEVEQLALP VATQGVADDK AALTLGDTSA VTADLDLPKT GSAGGSSISW
     ASDNPSVVSE TGKVTRPAAG EPDGRAELTA TLKKGTVTDT RSFDVTVLPA FDDETAARQA
     AEDLVVHNID DVRGNLTLPA DGSFGTHVTW SSAHPDVVAA DGTVHRPAHG AGAADVELTA
     TVTKGEATAT RTLTAKVPEL PAKQALKGYM FSYFTGEGTS DGEQLYAALS KGNDPLKWRE
     LNDGKPVLTS TLGEKGLRDP FIIRSPEGDK FYQIATDLRI YGNGDWDASQ RTGSKSIMVW
     ESTDLVHWTD QRLVKVSPDS AGNTWAPEAF YDEQRGEYVV FWASKLYDNE AHSGDTYNRM
     MYATTRDFHT FSEPKVWIDR GYSVIDSTVI QHGGTYFRLS KDERNNSSST PNSKFIFEEK
     SDSLLDTSWT PVAEGIGKGA MNAAEGPLVF KSNTEEKWYA FLDEFGGRGY IPFETTDLDS
     GVWTPSTGYD LPAKPRHGTV LPVTQAEYDR LLRAYQPDQL VDSVEDIAVK TRIGDAPVLP
     ATVIAKYADG VERPVSVDWA DVPESAYEQA GTFTVTGSLP EGGTLKAEVT VSAEGPDVPA
     DLLLDYDFDE TGGNIARDSS GHGYHGTYVR TPDFGTGVDG GSFKMSGGTS SSTTSPYVRI
     PNGVLKNADS VTVSTHVKWK GGDNFQWLFG LGPDSNKYLF ASPSNGGGKL FSAITEATWS
     GEKQMTAGSR LTPGEWQHVT VTVDSATETA VLYVNGIEAA RATGVTIKPS ELYDSSKGYS
     GYIGKSLYSP DPYFGGEVDD FRIYNRALAP TEVLELSGNT TGIAAATHPA LKTDAIIDDA
     AGKITLPLAE GSDLTALAPE FALAHGASIS PASGTLHDFT EPVTYEVTGS DGAKRTWKVT
     ALEMKSPVLP GLNADPNIVR FGDTFYIYPT TDGFPGWSGT QFKAYSSTDL VHWKDHGVIL
     DLGPDVSWAD SRAWAPTMAE KNGKYYFYFS ADANIGVAVS DSPTGPFKDP LGKPLLKAGQ
     LTGQMIDPAV FTDDDGTSYL YFGNGRAYVV PLNDDMTSLD STKIKDITPS GYNEGTFVIK
     RKGTYYFMWS ENDTRDENYR VAYATGSSPT GPWTKQGVIL EKDLSLGIKG PGHHSVVHVP
     NTDDWYIAYH RFAIPGGDGT HRETTVDKLE FDADGLIEKV VPTLTSIDPV TVVHAGSDAD
     GTEGDAIRIS GTLSGAGSPK WTIEKGAPCA FADAGAAATT LTCRDDGTYE VTLTGGRSSD
     TATVTVGNAA PAITSAHGPA SPVAANRATA VSAAFGDPGS ADTHTCTVDW KDGGEPTRGT
     VSDSRCTATH TYTTAGIRRP VVTVTDDDGA SDRRTLPELV VYDRAAGPAA GVGIVTSAAG
     AYPAQPGLTG KAAFSFTADY RRNADVPTGK VTFDFGAARL KFRSTGSDWL VVTKSRAVYQ
     GSGTVNGAAG YGFRITATDG PDTFRIEVWK KSTGAVVYDN ATAATVTGFV TVGGPRL
//
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