ID A0A0D0XBZ5_9ACTN Unreviewed; 449 AA.
AC A0A0D0XBZ5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:KIR66930.1};
GN ORFNames=TK50_12835 {ECO:0000313|EMBL:KIR66930.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR66930.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR66930.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR66930.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC galactose ester bond in pectin. Active against paranitrophenyl-acetate,
CC methyl ferulate and wheat arabinoxylan.
CC {ECO:0000256|ARBA:ARBA00025250}.
CC -!- SIMILARITY: Belongs to the faeC family.
CC {ECO:0000256|ARBA:ARBA00010278}.
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:KIR66930.1}.
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DR EMBL; JXSX01000001; KIR66930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0XBZ5; -.
DR ESTHER; 9actn-a0a1c4w365; FaeC.
DR PATRIC; fig|47853.6.peg.2714; -.
DR Proteomes; UP000032254; Unassembled WGS sequence.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 3.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR043595; FaeB/C/D.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR38050; -; 1.
DR PANTHER; PTHR38050:SF1; FERULOYL ESTERASE C; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIR66930.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032254};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..449
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002240948"
FT DOMAIN 35..171
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 449 AA; 47243 MW; EE24FAD7A8FBEDA4 CRC64;
MARVTAAAAA TVLVGGAVVA VNSTPAAAAT VDTGAWYVLL NRNSGKALDL YNLATNDGAR
ITQWTRNDGN QQQWQFVDSG GGYYRLKSRH SGKVLDVSGA STADGAAVVQ WSDVNGTNQQ
FRLADSADGY VRLIARHSNK AVEIQNASTA DGANVVQYAD WNGSNQQWQL VRVNGGTTPT
TPPPGNGTAG CGKAPGIASG THTISSGGKN RTFILRIPAN YHQSTPYRLV FGFHWWGGTA
VDVDTGQTVD RNTWSYYGLQ RLANNSTIFV APQGIDNGWA NAGGEDVTFV DNMLSRIEGA
LCVNPRQRFS IGFSYGGAMS FSLACSRPNI FRAVVVQSSP GTLSGCSGGT QPVAYLGVHG
IGDNPASGRA LRDRFVANNG CTPQSPREPS AGSLTHVVTT YSGCRSGYPV VWAAFDGGHI
AAPQDGAPGD SGPRTWVPAT AWSFITQFQ
//
