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Database: UniProt
Entry: C6LLM3_9FIRM
LinkDB: C6LLM3_9FIRM
Original site: C6LLM3_9FIRM 
ID   C6LLM3_9FIRM            Unreviewed;       652 AA.
AC   C6LLM3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:EET58487.1};
GN   ORFNames=BRYFOR_09571 {ECO:0000313|EMBL:EET58487.1};
OS   Marvinbryantia formatexigens DSM 14469.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Marvinbryantia.
OX   NCBI_TaxID=478749 {ECO:0000313|EMBL:EET58487.1, ECO:0000313|Proteomes:UP000005561};
RN   [1] {ECO:0000313|EMBL:EET58487.1, ECO:0000313|Proteomes:UP000005561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14469 {ECO:0000313|EMBL:EET58487.1,
RC   ECO:0000313|Proteomes:UP000005561};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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:EET58487.1}.
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DR   EMBL; ACCL02000031; EET58487.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6LLM3; -.
DR   STRING; 168384.SAMN05660368_03957; -.
DR   eggNOG; COG3507; Bacteria.
DR   Proteomes; UP000005561; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EET58487.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005561}.
FT   DOMAIN          434..632
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        38
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            151
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   652 AA;  73595 MW;  2F372E671697E1B7 CRC64;
     MESQYVYGGS ISGGGRCSGK EKIIMQVKNP ILRGFHPDPS IIRAGVDYYI ATSTFEWWPG
     IQINHSRDLV HWEICTYALQ DAGQVNLQGI GPSQGIWAPC LTYDKGIFYL AYTVVNSFYC
     NMYDTRNYLI TAENIMGPWS EPVPLHNMGF DPSLFHDTDG KKYMVSMVTD HRVPKKYAGR
     IVLQEYDPER KKLVGEIKEI YAASDIFLEG PHILKHDGWY YLVAADTGTG EGHGQSILRS
     RSIWGPYEMY KSPKCVRTRE GEAWSIMTTR HSPEYPLQKA GHADFVETPD GQWYAVYLCG
     RALENRNPAD AKKFPGVRRY PLGRETAIQK VYWTEDGWLE IDSESVLPDL VTEIAGAEAV
     RTMPEYETAD IAEKTPAEAA VEAALEQETA DTAENKPVEQ ALEPGAGDEA EDEPVKPVAE
     AAPEPGAAEI FCEREDFDGA DISPEFQSLR IPMTEEYVSL TARPGWLRMY GREGLASLFR
     QSLIARRRTE FVCSCSCKVE FEPQNFKQMA GLICMYDTEN YMYLHISRDE DCGKCITLLR
     AENKVYTYPV EPVPLPEDVP VFLKAEIHYD RIQFYYAAGT EDYQKIGPED DCSYMSDEAC
     RQGWFTGSML GICCQDLTGA GQYADFDFFT YNTEEEEKVR QPQISAAAGE VL
//
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