ID A0A1I2NKB0_9ACTN Unreviewed; 540 AA.
AC A0A1I2NKB0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Ricin-type beta-trefoil lectin domain-like {ECO:0000313|EMBL:SFG01731.1};
GN ORFNames=SAMN05421541_1455 {ECO:0000313|EMBL:SFG01731.1};
OS Actinoplanes philippinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=35752 {ECO:0000313|EMBL:SFG01731.1, ECO:0000313|Proteomes:UP000199645};
RN [1] {ECO:0000313|EMBL:SFG01731.1, ECO:0000313|Proteomes:UP000199645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43019 {ECO:0000313|EMBL:SFG01731.1,
RC ECO:0000313|Proteomes:UP000199645};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FONV01000045; SFG01731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2NKB0; -.
DR STRING; 35752.SAMN05421541_1455; -.
DR Proteomes; UP000199645; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; cd08998; GH43_Arb43a-like; 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; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Lectin {ECO:0000313|EMBL:SFG01731.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199645};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011577965"
FT DOMAIN 369..455
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 159
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 540 AA; 58598 MW; 15D21799C27EE793 CRC64;
MRILGALLAA VLLTAVPAVP ARAAAPPVTG NPDPVAHDPT LIKQGRWWYE IITGDSGTRT
YLPIRRSIDL VHWTYTGTVF DTPPAWVAEE LGVTPADFWA PDITWFDGEY HLYYAASSFG
TNDSVIGLAT TKSLDRPQWV DRGLVLRTTK GVDDVNAIDP DVSFDRAGNA YLAYGSFWDG
LRMRRLDTST GLLSTTDTTE HRIASRGGMA IEGPSITYHD GWYYLFVSFD FCCRGVNSDY
RVMVGRSRSI TGPYLDAAGK ALTEGGGTQI LAGYNDFAGP GHGDVYGDLF AHHYYDRADG
GAPKGSIRRI SWAHGWPRLS DPLSGNRGYG HGDAYVQLVH RDSRAVLANA SCGYEGADVT
LAAADRTNAC QQWQLIDRGD GLVSLTNRQS NKVAEVAACV DADGARVAQW GWLANDCQRF
RLTPSTGGWS RIVSPLAGRA LQPAGCGAAG AAVQTFPAGA CQDFRIQPVG DVLLTDVANT
TRIGDRWRFT HVSDGWYRIT GTLTHRTLGG TLWRIEALTT GGYRLTGENG RTREVLLLTP
//
