ID A0A1M7M793_9ACTN Unreviewed; 457 AA.
AC A0A1M7M793;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Poly(3-hydroxybutyrate) depolymerase {ECO:0000313|EMBL:SHM86596.1};
GN ORFNames=SAMN05216499_115124 {ECO:0000313|EMBL:SHM86596.1};
OS Actinacidiphila paucisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310782 {ECO:0000313|EMBL:SHM86596.1, ECO:0000313|Proteomes:UP000184111};
RN [1] {ECO:0000313|EMBL:SHM86596.1, ECO:0000313|Proteomes:UP000184111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2025 {ECO:0000313|EMBL:SHM86596.1,
RC ECO:0000313|Proteomes:UP000184111};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRBI01000015; SHM86596.1; -; Genomic_DNA.
DR RefSeq; WP_073500754.1; NZ_FRBI01000015.1.
DR AlphaFoldDB; A0A1M7M793; -.
DR STRING; 310782.SAMN05216499_115124; -.
DR ESTHER; 9actn-a0a1m7m793; FaeC.
DR OrthoDB; 9767239at2; -.
DR Proteomes; UP000184111; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184111};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..457
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039616730"
FT DOMAIN 328..456
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 303..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 47499 MW; 6A025ECD3C511D9C CRC64;
MRRRSLLPAV LAALAMVLAA VGISLSGFSA TAWSAPNAAT GGCGKAPTLA SGTHTITSSG
QNRSYILRVP ANYDQNHPYR LVFGFHWVGG TANDVDSGGT DGYNWSYYGL RRLADSDGNG
TVFVAPQGIS NGWANSNGQD VTFVDDMLRQ LEGGLCVDTG QVFSSGFSYG GSMTYALACA
RPTVFRAVAV YSGANLSGCS GGTQPVAYIG LHGIRDNVLP ISSGRALRDT FVRNNGCTPQ
NPPEPANGSL THIVTAYSGC KAGYPVVWAA FDGAGHDPGP IDGSTGDGWH TWTSGVVWNF
FSQFSSSTPP TTPPTTPPTT PPTTPPPSGS QQIVGQQSGR CLDIGNSSTT NGTQAELWDC
NGGTNQRWAY SASKQLVVYG NKCLDASGQG TANGTAAVIW DCNGQPNQQW NLNANGTITG
VQSGLCLDAA GTGTANGTKI QLWACTGGAN QQWSERN
//
