ID G8SM80_ACTS5 Unreviewed; 443 AA.
AC G8SM80;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Poly(3-hydroxybutyrate) depolymerase {ECO:0000313|EMBL:AEV87059.1};
DE EC=3.1.1.72 {ECO:0000313|EMBL:AEV87059.1};
GN OrderedLocusNames=ACPL_6174 {ECO:0000313|EMBL:AEV87059.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV87059.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) 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}.
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DR EMBL; CP003170; AEV87059.1; -; Genomic_DNA.
DR RefSeq; WP_014693127.1; NZ_LT827010.1.
DR AlphaFoldDB; G8SM80; -.
DR STRING; 134676.ACPL_6174; -.
DR ESTHER; acts5-g8sm80; FaeC.
DR KEGG; ase:ACPL_6174; -.
DR PATRIC; fig|134676.3.peg.6064; -.
DR eggNOG; COG3509; Bacteria.
DR HOGENOM; CLU_027551_2_1_11; -.
DR OrthoDB; 9767239at2; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
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; PF00652; Ricin_B_lectin; 1.
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:AEV87059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..443
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003517158"
FT DOMAIN 314..442
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 305..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 45640 MW; BF27F71B4B1F8E66 CRC64;
MVRKRLAVLA AVISGALGLA LAGALPSDAF ATSAAAPTAG CGQAPTLAGG THTISSGGQN
RSYILRIPAG YDGNHPYRLV FGFHWNGGTA GDVDSGGTDG YNWSYYGLRR LADAAGNGTI
FVAPQGIGNG WANSGGRDLT FVDDMLRQIE GGLCVDTSQI FSSGFSYGGA MSYALACARP
TVFRAVAVYS GGNLSGCISG TQAVAYIGLH GLRDNVLPIS SGRALRDTFV RNNGCTPQNP
PEPANGSLTH IVTTYSGCRA GYPVVWAAFD GAGHDPGPRD GCTCDGWQTW TSGVVWTFFA
QFGGGTPPSS PAPGGARQLV GEQSGRCADV PNSSTANGTQ VQLWDCSGTA GQRWTWTSGR
QLQVYGTKCL DANGQGTANG TAVIIWDCNG QANQQWNVTA NGTVTGQQSG LCLDANGAGT
ANGTRLILWA CNGGANQRWS LRG
//
