ID A0A2U2ZLY3_9ACTN Unreviewed; 1733 AA.
AC A0A2U2ZLY3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:PWI13286.1};
GN ORFNames=DI272_03420 {ECO:0000313|EMBL:PWI13286.1};
OS Streptomyces sp. Act143.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI13286.1, ECO:0000313|Proteomes:UP000245455};
RN [1] {ECO:0000313|EMBL:PWI13286.1, ECO:0000313|Proteomes:UP000245455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Act143 {ECO:0000313|EMBL:PWI13286.1,
RC ECO:0000313|Proteomes:UP000245455};
RA Valanrebinro G., Kumari S., Rameshkumar N.;
RT "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT of saline tolerant kaipad rice and its draft genome analysis.";
RL Submitted (MAY-2018) 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:PWI13286.1}.
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DR EMBL; QFRX01000001; PWI13286.1; -; Genomic_DNA.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000245455; 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; 2.60.40.2340; -; 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; 1.
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:PWI13286.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000245455};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..1733
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015638678"
FT DOMAIN 908..1049
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1153
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 1312
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 1265
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 1733 AA; 183344 MW; 52B0D70C75014B65 CRC64;
MTHLARPRTR ARRRAGRLAG LTAVSLFLGL TAPVTSATAA TAAGTADVTD GLALWYKLDA
ASGSTVTDAS GNGRDGTVNG TADWSDTGQG LAFNGSDTYV KVPNDVMKGM TAITVSTDVL
IDSAQTTPYF IYGFGNSSGS SGNGYLFTTG NSLRTSIATG NWSTEQTTRP ADSHNLTRAV
WKHLTYTQTG STGILYEDGV EVGRNTSVST TPGAIGSGTT TANYIGKSVY SGDKLFKGRI
RDFRVYDRAL DAAEVEQLSL PVATQGVADD KAALDLGDTS AVTADLDLPK TGTAGGSTIS
WASDNTAAVS DTGKVTRPAA GAPDAHATLT ATLKKGTVSD TRTFAITVLP DFDDKTATEQ
AAQALTVHNL DDVRGNLTLP ADADHGTKVA WSSANPDVIT ADGVVHRPAH GDGATTVELT
ATVTKGTAST TRTFTAEVPE LPAKQALKGY MFSYFTGEGT ADGEQLYAAL SKGDDPLKWR
ELNDGKPVLT STLGEKGLRD PFIIRSPEGD KFYQIATDLR IYGNGDWDAA QRSGSKSIMV
WESTDLVHWT NQRLVKVSPD SAGNTWAPEA FYDAERGEYV VFWASKLYDN EAHSGDTYNR
MMYATTRDFY TFSEPKVWID RGYSVIDSTM IRHDGTYYRL SKDERNNTSS TPNSKFIFEE
KSDSILGSWT AVAEGIGKGA MSAAEGPLVF KSNTEEKWYA FLDEFGGRGY LPFETTDLDS
GVWTPATDYD LPAKPRHGTV LPVTQAEYDR LLRAYQPDQL VESVESVDVQ TRTGEAPVLP
ATVIATYADG VKRPVAVTWE DVPASKYAQP GTFTVTGSLP DGAALPVRAE VTVSQEGPDV
PADLLLEYDF DEAGGNIARD ASGHGHHGTY VRTPAFGTGV DGGSFKMSGD SATSPYVKIP
NGVLKNAGSV TVSAYAKWQG GASFQWLFGL GPDSDKYLFA TPSNGGSSLY SAITKASWSA
ESKLTAGSQL TPGEWRHVTV TLDGTTGTMV LYVDGIEAAR TTTGITPSEL YDANKDYSGY
IGRSLYAADP YFGGEVDDFR IYDRALTAAE VMELSGNTAG IAKATQTGLK VDAIIDNAGG
RITLPMTEGT DLTALAPEFT LAHGAAISPA SGSVQDLSKP VTYEVTGSDG KKRTWTVAAL
VMKSPVLPGL NADPNIVRFG DTFYLYPTTD GFEGWSGTQF KAYSSTDLVH WKDHGVILDL
GPDISWADSR AWAPTIAEKD GKYYFYFCAD ASIGVAVSDS PTGPFKDALG QPLLKAGQFS
GQMIDPAVFT DDDGTSYLYW GNGHAYVAPL NADMVSLGTA KTKDITPGGY NEGSFVIKRK
GTYYFMWSEN DTRDENYRVA YATGPSPTGP WTKRGVILEK DLSLGIKGTG HHSVVHVPGT
DDWYIAYHRF AVPGGDGTHR ETTVDKMEFD ADGLIKKVVP TLTGIDPVTI VHAGPDAEGT
EGEAVALHGT LSGAGSPKWT AEDGAPCTFA EPAAARTTVT CTDDGTYTLT LTGGRSSDTA
TVKTANAAPA VTSATGPESA VSVGRTAVVT AAFTDPGGSD THTCTVEWKD GGAPQPGRIT
ATGCRAEHTY TKAGIRRPVI TITDDDGASD ATTLPELVVY DRAAGPVFGT GVFTSPAGAC
PARPDLTGKA AFSFVARYEK GAAVPTGWAS FDFGPARLKF RSTGSDWLVV TGSQAVYQGS
GTVAGAGGYA FRVTATTDSY RIRIWKKAGG DVGYDNATSP KMAGIITFGT ARG
//
