ID G8SA03_ACTS5 Unreviewed; 415 AA.
AC G8SA03;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=CBM2 domain-containing protein {ECO:0000259|PROSITE:PS51173};
GN OrderedLocusNames=ACPL_3011 {ECO:0000313|EMBL:AEV83906.1};
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:AEV83906.1, 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; AEV83906.1; -; Genomic_DNA.
DR RefSeq; WP_014689978.1; NZ_LT827010.1.
DR AlphaFoldDB; G8SA03; -.
DR STRING; 134676.ACPL_3011; -.
DR ESTHER; acts5-g8sa03; FaeC.
DR KEGG; ase:ACPL_3011; -.
DR PATRIC; fig|134676.3.peg.2931; -.
DR eggNOG; COG3509; Bacteria.
DR HOGENOM; CLU_027551_2_1_11; -.
DR OrthoDB; 9767239at2; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR043595; FaeB/C/D.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR38050; -; 1.
DR PANTHER; PTHR38050:SF1; FERULOYL ESTERASE C; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..415
FT /note="CBM2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003515746"
FT DOMAIN 312..415
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 415 AA; 42198 MW; 324FB39DC3EDBC4A CRC64;
MTRRTVTAIL CALALATATL TGLFGTGVPA TAAVAGCGKA PTLTSGTRTI SSGGQNRTYI
LRVPDGYDRN HPYRLMFAFH WLNGTAADVA TGGPAGATWA YYGQQRLAGA TTILVAPQGI
DNGWANPGGR DLALVDALTA LIEGDLCVDT SQVFALGWSY GGAMSYAVAC ARPAVFRAVA
VLSGANLSGC SGIGQPVAYL GIHGIHDSVL DISLGRGLRD SFVRANGCTA QNPPEPARGS
LTHVVTAYTG CRTGHPVEWA AFDGDHTPEP VDGTTATDGA RTWTGAEIAK FFAQLPSTTP
PVSPSVTPSG TPGGQPGGCA VTYRVVNSWP GGFQAEVTVT NTGTTPTSGW RVGWTLPAGQ
SISQVWSGSL SVSGNAVTVV NATYNGMLDP GAAATFGLIA SGSPAITPAI ACTLP
//
