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Database: UniProt
Entry: R6EBT4_9BACT
LinkDB: R6EBT4_9BACT
Original site: R6EBT4_9BACT 
ID   R6EBT4_9BACT            Unreviewed;       453 AA.
AC   R6EBT4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Glycosyl hydrolase family 43 {ECO:0000313|EMBL:CDA94764.1};
GN   ORFNames=BN487_01125 {ECO:0000313|EMBL:CDA94764.1};
OS   Prevotella sp. CAG:1320.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262922 {ECO:0000313|EMBL:CDA94764.1, ECO:0000313|Proteomes:UP000018111};
RN   [1] {ECO:0000313|EMBL:CDA94764.1, ECO:0000313|Proteomes:UP000018111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1320 {ECO:0000313|Proteomes:UP000018111};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDA94764.1}.
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DR   EMBL; CBCU010000053; CDA94764.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6EBT4; -.
DR   STRING; 1262922.BN487_01125; -.
DR   Proteomes; UP000018111; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd18618; GH43_Xsa43E-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF6; -; 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51175; CBM6; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018111};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..453
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004404463"
FT   DOMAIN          324..450
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   ACT_SITE        32
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            147
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   453 AA;  50474 MW;  ADF6BDBD48356BB9 CRC64;
     MLRHKILCSL LAMSPLAGMA QNPIVQTMYT ADPAPMVSGD RLFLYTSHDE DNSTWFVMNN
     WKLYSTTDMV NWTDHGVVLS LKTFDWAQSD AWAMQCVERD GKYYAYVPVT KKGGGGAIGV
     AVADSPYGPF YDPLGKPLVS SGRGDIDPSV MIDEDGQAYL YWGNPFCYYV KLNEDMISYS
     GDIVRVPMTE EAFGKREGNV EERPTRYEEG PWLYRHDKWY YLLWAGGPIS EHLGYSMSKS
     PTGPWKNCGT LMPTEGRSFT NHPGIVDYKG NTYLFYHNGA LPGGGGFTRS VCVEQAEFNK
     DGTIKPMKMT AGITKGLGTL NPYRKTEAET MAFSEGMKGA QNEEVGVYVN AMKDGAYVKV
     RDVDFREAGP AKVTARVGTT HNGGVTMEVR VDNPQGPLLA TLKVPMTGWD DRWAVVSADV
     SKVSGVHDLY FVCRGDKPGR LMYFDYWMFS QNK
//
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