ID R6K8H2_9BACE Unreviewed; 356 AA.
AC R6K8H2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Glycosyl hydrolase family 43 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN506_01294 {ECO:0000313|EMBL:CDB69785.1};
OS Bacteroides cellulosilyticus CAG:158.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1263038 {ECO:0000313|EMBL:CDB69785.1, ECO:0000313|Proteomes:UP000018191};
RN [1] {ECO:0000313|EMBL:CDB69785.1, ECO:0000313|Proteomes:UP000018191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:158 {ECO:0000313|Proteomes:UP000018191};
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:CDB69785.1}.
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DR EMBL; CBEB010000027; CDB69785.1; -; Genomic_DNA.
DR AlphaFoldDB; R6K8H2; -.
DR Proteomes; UP000018191; 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:UniProtKB-KW.
DR CDD; cd18618; GH43_Xsa43E-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
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:UP000018191};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 168
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 356 AA; 39783 MW; 763C13D5727C4228 CRC64;
MRNTLFIASL YLILSACGEK SNEVKFTSEG NPVVMDKFTS DPAPMVHNGR LYLYVGHDEA
EEGQDFNITE WLCYSTKDMK TWTDHGSVLK PTDFSWGVGE AWASQVVEKD GKFYYYTTVQ
AGAPYNSKVV GVAVSDSPTG PFIDARGTPL ITDDMTPNGP RGWWNDIDPT VFVDDDGTPW
MSWGNGTCFL VKLKPNMTEL DGNIEILKMP KFVEGPWIHK RENLYYLTYA SMGKGRETIS
YATAPSMEGP WTYRGVLTGM AENSFTIHPG IIEFKGQSYL FYHNAILTID GKSGATGRRS
VCVDYLYYLP DGRMAYVEQT KEGITVKPKT AAEVAEIVNP YTDEKEVVVE KEVIAD
//