ID A0A2T6FN93_9GAMM Unreviewed; 563 AA.
AC A0A2T6FN93;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=CBM2 domain-containing protein {ECO:0000259|PROSITE:PS51173};
GN ORFNames=B0W54_05075 {ECO:0000313|EMBL:PUA29917.1};
OS Cellvibrio sp. 79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1954207 {ECO:0000313|EMBL:PUA29917.1, ECO:0000313|Proteomes:UP000243979};
RN [1] {ECO:0000313|EMBL:PUA29917.1, ECO:0000313|Proteomes:UP000243979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=79 {ECO:0000313|EMBL:PUA29917.1};
RA Zhang Y., Xu J., Wang N.;
RT "Cellvibrio sp. 79 recovered from metagenome.";
RL Submitted (FEB-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PUA29917.1}.
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DR EMBL; MVDH01000001; PUA29917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6FN93; -.
DR ESTHER; 9gamm-a0a2t6fn93; FaeC.
DR Proteomes; UP000243979; Unassembled WGS sequence.
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; 2.60.60.40; -; 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; IPR018366; CBM2_CS.
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.
DR PROSITE; PS00561; CBM2_A; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000243979};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 32..136
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 303..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 58852 MW; F73DEB9EDD28CBF6 CRC64;
MNKSKILPDG NLHKIKQSLL NVGIATTIVS AAHTASAACT YQIDNEWSNG FVASITVKND
TGAAVNNWSV NWQYANNRIT NSWNANLSGS NPYTATNLNW NGSIAAGQSV SFGFQGNKNG
NSAERPPING TLCSAAPVSS VASSSPVSSV RSSSSVAVVS SSQISSSVAL SSSSRVASSV
PTGTRNAITV RALGTTATES ITLSVGGTEV QSWALSTVMT NYTVETALVG DVVVTFANDD
GGNADVRIDY VNVNGVTRQA EVQTENTGAW GNNRCGGGAP SEWLHCEGYI NFGSVTGEPR
SSSSVASSIS SVSSSSSSRT GAGSAGCGAP AKLTNGRRTI NVNGLNREYV LDIPSNYNQN
NPYKLVFGWH WRGGSANDVV SQGYYGMKSL SNNSAIFVAP DRAAGTDGWT NANGRDIAFL
QSMLTQLKSS LCIDESRIFS TGWSYGGMMS FAVGRELPST FRAIAPVSGA FLTPHVDSGS
ATAAWIAHGT SDNVVSHSSG AQARDAYLRA NGCSNTTVPV QPSPCVEYQN CSSGKPVVWC
SFNGGHTQPS FYSSGAWNFF NRF
//
