ID R5I5A4_9BACT Unreviewed; 471 AA.
AC R5I5A4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Oxidoreductase NAD-binding domain protein {ECO:0000313|EMBL:CCY37278.1};
GN ORFNames=BN796_00874 {ECO:0000313|EMBL:CCY37278.1};
OS Alistipes sp. CAG:831.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1262698 {ECO:0000313|EMBL:CCY37278.1, ECO:0000313|Proteomes:UP000018094};
RN [1] {ECO:0000313|EMBL:CCY37278.1, ECO:0000313|Proteomes:UP000018094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:831 {ECO:0000313|Proteomes:UP000018094};
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 -!- 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:CCY37278.1}.
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DR EMBL; CAYB010000142; CCY37278.1; -; Genomic_DNA.
DR AlphaFoldDB; R5I5A4; -.
DR STRING; 1262698.BN796_00874; -.
DR Proteomes; UP000018094; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000018094};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..471
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004381791"
FT DOMAIN 64..189
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 200..342
FT /note="Glycosyl hydrolase 109 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21252"
SQ SEQUENCE 471 AA; 53038 MW; 531D60690FA10002 CRC64;
MKLRHLAIAM TAALGMAASC DTVQHCDSSI PYDIQDGKIV FQVPPRIEGQ KSVLGLTTEP
METVRVGFIG LGMRGPGAVE RFTHIEGTEI KALCDLYPER AAAAQEILKK AGRPHAQEYS
GEEGWKELCQ RDDIDLVYIV TPWQKHVEMA VFAMEQGKHV AIEVPAATSL AECWELVNTA
ERTQRHCMML ENCVYDFFEM TALNMAQQGL FGEVLHGAGG YIHNLEPYWD EYQGNWRLDF
NQDHRGDVYA THGFGPICQA MNIHRGDRLQ TLVAFDTKSV NGLKLVQEKM GLDECANGDY
TITLMRTANG KMIEVHHNVM TPRPYDRKYQ LTGTEGFANK YPIEGFTFMP ENIDTDEVPD
HEDLNAHGFV PEAARKALME KYMHPIHREV GEIAKKVGGH GGMDFVMDYR LVYCLRNGLP
LDMDVYDAAE WSCVGELGAV SMFHGNMPVE VPDFTRGDWD KTDGFHFAYK K
//
