ID E2NG50_9BACE Unreviewed; 422 AA.
AC E2NG50;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Oxidoreductase, NAD-binding domain protein {ECO:0000313|EMBL:EEF89115.1};
GN ORFNames=BACCELL_03272 {ECO:0000313|EMBL:EEF89115.1};
OS Bacteroides cellulosilyticus DSM 14838.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=537012 {ECO:0000313|EMBL:EEF89115.1, ECO:0000313|Proteomes:UP000003711};
RN [1] {ECO:0000313|EMBL:EEF89115.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF89115.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF89115.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF89115.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838).";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000256|ARBA:ARBA00009329}.
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:EEF89115.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACCH01000231; EEF89115.1; -; Genomic_DNA.
DR RefSeq; WP_007212628.1; NZ_JANSWE010000056.1.
DR AlphaFoldDB; E2NG50; -.
DR HOGENOM; CLU_046965_0_0_10; -.
DR Proteomes; UP000003711; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR049303; Glyco_hydro_109_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF1; GLYCOSYL HYDROLASE FAMILY 109 PROTEIN; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF21252; Glyco_hydro_109_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 20..143
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 157..318
FT /note="Glycosyl hydrolase 109 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21252"
SQ SEQUENCE 422 AA; 47196 MW; 219FD234EE9EE474 CRC64;
MKNEPPTHVL GLAHPPIPVV RIGLIGLGNR GLLTLERYML IEHVEIKALC EIRPGNLAKG
QALLTKGGHP AATGYAGENG WQQMCCNPDI DLIIICTDWL THTPMATYAM EQGKHVAIEV
PAAMTVAECW QLVNTAERTR RHCIMLENCC YDAFALTTLN MARQGLFGEI MHVEGAYIHD
LRSMYFSDEN QGGFHNHWNK AYCMEHTGNP YPTHGLGPVC QILNIHRGDR LNYLVSMSTH
QAGMTEYARR TFGKESPEAQ QAYLLGDMNT TLIHTVKGKT IQLQYCTVHP RPYSRSHTIC
GTRGFAQKYP VATISLEDVR SGEADSATTE ELLQRYQHPF TATIGKEGAL KGAPNEMNYI
MDYRLIYCLH HGLPLDMDVY DAAEWSCITE LSEQSVLNGS RPVEIPDFTR GAWETFPCVA
KN
//
