ID U5VV25_9ACTN Unreviewed; 469 AA.
AC U5VV25;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:AGZ40853.1};
GN ORFNames=AFR_12835 {ECO:0000313|EMBL:AGZ40853.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ40853.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ40853.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ40853.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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; CP006272; AGZ40853.1; -; Genomic_DNA.
DR RefSeq; WP_023360912.1; NC_022657.1.
DR AlphaFoldDB; U5VV25; -.
DR STRING; 1246995.AFR_12835; -.
DR KEGG; afs:AFR_12835; -.
DR PATRIC; fig|1246995.3.peg.2607; -.
DR eggNOG; COG3940; Bacteria.
DR HOGENOM; CLU_009397_2_0_11; -.
DR OrthoDB; 5240321at2; -.
DR Proteomes; UP000017746; Chromosome.
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; cd18820; GH43_LbAraf43-like; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..469
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004665248"
FT DOMAIN 341..469
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 325..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 154
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 469 AA; 49906 MW; 44C4F6F8578D48EF CRC64;
MAVVAVLLAG LALVVADAPQ PARAAGTFVN PVSPRPDPFV VFHRGRYYTV ENDTSETRLL
IRSAATVAGL SAATPQLVWA DGNTSRNKQV WAPSLLNLND RWYLYYTASD GVDNNHRNYV
LESTGLVSQG ATPAGPYAFK ARIFDPAADS WAIDGLPFTH NGALYYAYAG ALGNQHNEMF
IARMANPYSL SGARTHLPLA GGCPTIREAP ATLNRNGRTW LVYSTCDTGT PDYQLWMTSI
ADGADPLVAT NWRQRSGAVY QRNDAAGVFA PGSNNFFRSP DGTEDWMAYH AKTTSAFTYD
GRTTRLQKIG WNTDGSPDLG RPIALGTAQA TPSGDPGPSA PAAGTRIAGP GGKCVDVAGD
DTGANLSPVQ LWDCLGAAAD QLWTWNGTSL RTLGRCLDVA GNITAAGTRL QLWDCNGAGG
QQWVQQANGS MLNPQSGRCL DSPSGATANG TRLQIWDCNG SPAQVFRKQ
//
