GenomeNet

Database: UniProt
Entry: D9UKP3_STRS3
LinkDB: D9UKP3_STRS3
Original site: D9UKP3_STRS3 
ID   D9UKP3_STRS3            Unreviewed;       757 AA.
AC   D9UKP3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Arabinan endo-1,5-alpha-L-arabinosidase A {ECO:0000313|EMBL:EFL03701.1};
GN   ORFNames=SSLG_05759 {ECO:0000313|EMBL:EFL03701.1};
OS   Streptomyces sp. (strain SPB78).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=591157 {ECO:0000313|EMBL:EFL03701.1, ECO:0000313|Proteomes:UP000005781};
RN   [1] {ECO:0000313|EMBL:EFL03701.1, ECO:0000313|Proteomes:UP000005781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPB78 {ECO:0000313|EMBL:EFL03701.1,
RC   ECO:0000313|Proteomes:UP000005781};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain SPB78.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG657742; EFL03701.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9UKP3; -.
DR   STRING; 591157.SSLG_05759; -.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_388142_0_0_11; -.
DR   Proteomes; UP000005781; 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:InterPro.
DR   CDD; cd18616; GH43_ABN-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          554..722
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            156
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   757 AA;  79536 MW;  9EE1D0907BCD8AE2 CRC64;
     MPPAGRAHAA EAGVRHGAAP ATYTNPVSGQ AVDTFPDPAM IRGKDGYWYA YGTQNPVFQS
     KGETGERMLP ILRSADLTHW TYAGEVFTPA DQPAWHGGSR LWAPDIRYTD GQYTLYYSVP
     DRNTVGVATA PTPTGPWTDR GAVLPSPSGC ASGNIDQAQF TDVGGQPYLY WGSYDTICVA
     RLNGDRTRVE GQVTEVAQGR RVEGGFVVRR EGWYYLFYSD AGCCDGGASG YQVKVGRSQS
     PTGPFSDDQG VPLMAASSKG TVVVGGDGRW IGAGHNALQT DLSGQDWLVY HAIPAADPDL
     ARVPGIDRTL SRRPLLIDRL DWIDGWPVVR AGAGPSHDAQ PAPVTAWDTG STFASGGLDG
     WQARGADTGA WALGSDRDAG GLVSRTGAGR EAGYLVSPGT APARVRAEAD LRVTAAGGSA
     GLVLAHQDAG DQIVAWLDRP TNSLVTDVLV NGRSAGRRST PLPSGFQWGA WRNVAAELRG
     TRLTVEVSAD RLHDAVATQT RTVPDSAVRA GHVGIAARGA GAQADNVGGV RLYTPVTERV
     PDPRTGPQLS LYGDEFDGPA PNSGWSWVRG PATGAGTSGG DFVLPTQNAE LNLGTNTASV
     LNRPAPSGDF VVETKLSIAN GPGNQQAGLV LYGGDDRYVK LVHAVLPVSH KDGQVTHVTE
     FAREGALPAA RPPAANAYGP MFGGAPGATV WLRLARHVDT ARDLHEVRAA ISTDGTHWTW
     TGTWTLPDAS APLRIGLVAL NTAGATARFG YVRTYAG
//
DBGET integrated database retrieval system