ID C9ZEB0_STRSW Unreviewed; 494 AA.
AC C9ZEB0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Putative arabinofuranosidase {ECO:0000313|EMBL:CBG74901.1};
GN OrderedLocusNames=SCAB_79411 {ECO:0000313|EMBL:CBG74901.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG74901.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG74901.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG74901.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
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DR EMBL; FN554889; CBG74901.1; -; Genomic_DNA.
DR RefSeq; WP_013005351.1; NC_013929.1.
DR AlphaFoldDB; C9ZEB0; -.
DR STRING; 680198.SCAB_79411; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH54; Glycoside Hydrolase Family 54.
DR GeneID; 24312452; -.
DR KEGG; scb:SCAB_79411; -.
DR eggNOG; COG2755; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_029332_4_0_11; -.
DR OMA; YWRDGHL; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR GO; GO:0031221; P:arabinan metabolic process; IEA:InterPro.
DR GO; GO:0019566; P:arabinose metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR InterPro; IPR038964; ABFB.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR39447; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..494
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003005411"
FT DOMAIN 41..166
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 451
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 178..188
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 238..243
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 331..332
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 494 AA; 50666 MW; D74A775B85C1F6C5 CRC64;
MVFRIPRPRW YGRLSALGTA LVLVAVGATA VAAPIEPGQS APLVGAQSGR CLTVPGASTT
NGTQTQLQDC TGTTGQTWTY TTGRQLTVPG NKCLDASGSG TTNGTPVIIW DCNGGTNQQW
NVNPNGTITG VQSGLCLDAN AGGTANGTRT ILWSCHGGTN QQWNSPPDPP EPGDGGTCDI
YASGGTPCIA AHSTVRALYG TYSGNLYQVR RSSDSTTRNI GVRSAGGAAD AAAQDSFCAG
TACVITVVYD QSGRGNDLWY QGSSVVPGSP QSRPATATSE SLTVGGSKAY SLYINPGNSY
WRDGHLTGVP TGSAPEGMYM VTSGTHVNGG CCFDYGNSET TRAADAAGAM DAINFSTQCW
FGGCVGRGPW VQADLEWGLY SGGSQSWNTN QRAFTGKFVT AMLKNNGTSR FALRGADAQT
GGLTTLWDGA LPPGYSPMKK QGAIILGSGG DCCKPGGGAN LSAGTFYEGA MVSGYPSDAT
DNAVQANIVA AGYR
//