ID C7Q329_CATAD Unreviewed; 461 AA.
AC C7Q329;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Ricin B lectin {ECO:0000313|EMBL:ACU73765.1};
DE Flags: Precursor;
GN OrderedLocusNames=Caci_4905 {ECO:0000313|EMBL:ACU73765.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU73765.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU73765.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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; CP001700; ACU73765.1; -; Genomic_DNA.
DR RefSeq; WP_015793494.1; NC_013131.1.
DR AlphaFoldDB; C7Q329; -.
DR STRING; 479433.Caci_4905; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR ESTHER; catad-c7q329; FaeC.
DR KEGG; cai:Caci_4905; -.
DR eggNOG; COG3509; Bacteria.
DR HOGENOM; CLU_027551_2_1_11; -.
DR InParanoid; C7Q329; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; 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 Lectin {ECO:0000313|EMBL:ACU73765.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT DOMAIN 332..461
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 309..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 47364 MW; A6E3CE70CA972570 CRC64;
MQKRRAVFGP VALMALLVAL VSALTVYGGL GAASASPGAA PAAASSGCGK APVLASGSHT
IQSSGQNRSY ILRLPANYDS SHPYRLVFGF HWVGGTDNDV DSGGTDGYNW SYYGLRKLAD
ADGNGTIFVA PQGINNGWAN SGGQDVTFVD DMLSQFESGL CLDTSQVFSS GFSYGGSMTY
ALACARPAVF RAVAVYSGAN LSGCAGGTQP VAYIGLHGIR DNTLPIANGR ALRDTFVRNN
KCTPQNPPEP AYGSLTHIVT AYSGCLPGYP VVWAAFDGAG HDPGPIDGST GDGWHTWTSG
VVWNFFTQFQ NGQPPSSTPS TPPSTTPPGN GQGALHAIGA GKCLDDPNSA TTTGTQLQIH
DCTGQANQAW THTSSGQLSV TVGGSTLCLD ANGKGTTNGT KAILWSCNGQ SNQQWTLNSN
GTVTGAQSGL CLDVTGASSA NGALVELWTC NGGSNQQWAL S
//
