ID A0A0C5VIM8_9GAMM Unreviewed; 426 AA.
AC A0A0C5VIM8;
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=Poly(3-hydroxybutyrate) depolymerase {ECO:0000313|EMBL:AJQ93198.1};
GN ORFNames=YC6258_01150 {ECO:0000313|EMBL:AJQ93198.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ93198.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ93198.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ93198.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) 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; CP007142; AJQ93198.1; -; Genomic_DNA.
DR RefSeq; WP_052830069.1; NZ_CP007142.1.
DR AlphaFoldDB; A0A0C5VIM8; -.
DR STRING; 1445510.YC6258_01150; -.
DR ESTHER; 9gamm-a0a0c5vim8; FaeC.
DR KEGG; gsn:YC6258_01150; -.
DR HOGENOM; CLU_027551_2_2_6; -.
DR OrthoDB; 7053703at2; -.
DR Proteomes; UP000032266; Chromosome.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; 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; IPR001375; Peptidase_S9.
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; PF00326; Peptidase_S9; 1.
DR Pfam; PF14200; RicinB_lectin_2; 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:UP000032266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..426
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002183719"
FT DOMAIN 23..160
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 161..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 46287 MW; 3ABAB349DE1B7F9E CRC64;
MFKKIICCTV LMLFYSSAQA IENGRYNIVS SLNGLYLDVA NKSQDDGANI QQYTATGGTN
QQFDVTALGD GTYSIRAVHS GKSLDIAGYS MDDGAQVHQW TYHGGDNQRW YIDVAANGFY
SVTSKLSSKA LDVWEMSTQP GGDIRMYSWW GGAGQLWSFL PVGGGDPTDP TDPTDPPAGT
DPSAGCGNVP SLSSGRHSIN VNGATREYIL DVPANYDMSK PYRLIFGWHW LNGNASNVAN
GGYYGLKNLA NNSAIFVAPD RYVANGQDDN GWPNTNGRDM AFLRAMLDQF NNSLCVDKSR
VFSVGWSYGG MMSYAVGREM GGVFRAIAPM SGALWTPYND SGKPMPAWIA HGIYDSVVSH
DNGITARDLY VSANHCSNNT VPVDPSPCVE YQGCDAGYPV VWCSWNGGHS TPSFSPTAIW
TFFNRF
//
