ID A0A087CG07_9BIFI Unreviewed; 543 AA.
AC A0A087CG07;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Beta-1,4-xylosidase {ECO:0000313|EMBL:KFI82207.1};
DE EC=3.2.1.37 {ECO:0000313|EMBL:KFI82207.1};
GN ORFNames=BPSY_1056 {ECO:0000313|EMBL:KFI82207.1};
OS Bifidobacterium psychraerophilum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=218140 {ECO:0000313|EMBL:KFI82207.1, ECO:0000313|Proteomes:UP000029050};
RN [1] {ECO:0000313|EMBL:KFI82207.1, ECO:0000313|Proteomes:UP000029050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21775 {ECO:0000313|EMBL:KFI82207.1,
RC ECO:0000313|Proteomes:UP000029050};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KFI82207.1}.
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DR EMBL; JGZI01000009; KFI82207.1; -; Genomic_DNA.
DR RefSeq; WP_033495041.1; NZ_JGZI01000009.1.
DR AlphaFoldDB; A0A087CG07; -.
DR STRING; 218140.BPSY_1056; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000029050; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09000; GH43_SXA-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000029050}.
FT DOMAIN 335..537
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 127
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 543 AA; 61863 MW; C25AA4388A70003F CRC64;
MRISNPVLRG FNADPSMIRV GDTYYIANST FEWWPGVRLH ESQDLVHWRP LPAPLNRVSQ
LDMRGVPSSG GVWAPDLSYA DGRFWLVYGD VKVVNGAFKD CTNYLVTADD IHGPWSEPIR
VNGVGFDASL FHDDDGRKYL IQQTWDFREY HHPFDGITLT EFDTQGMRLM PETARTIWRG
TDVKTVEGPH LYKLNGYYYL FAAEGGTMFE HQESVARSRT LDALSFEVMP GNPLLGNYDT
PDSYLQKQGH GALVDTPSGE WYYASLCARP WRHDTEPSRG VRGWCPLGRE TSIQKIEWDD
ALWPRVVGGR GGSRYVQAPR DAIETIVPAD ASQHDEFDDH ELGRDWNTLR VPFGDAMGTV
GEGSLELRGQ GSLGNLFDLS LVARRWQTYT FDATVELSFK PDCYMQMAGL TNYYNDLCWS
WIFVTWDERR SKRVIEVAQN DFNAYTSFLR DRAIEIPDEV GSVWFRTSIR KRSYAYAYSF
DGTSWKDIPL VFDAKKLSDD YVSQRYGGFF TGAFVGLAAV DLAGFGKTAS FRHFDYREIP
DPA
//
