ID R5LXJ2_9BACT Unreviewed; 297 AA.
AC R5LXJ2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Dihydrofolate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN473_00635 {ECO:0000313|EMBL:CCY83928.1};
OS Prevotella sp. CAG:1185.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262921 {ECO:0000313|EMBL:CCY83928.1, ECO:0000313|Proteomes:UP000018054};
RN [1] {ECO:0000313|EMBL:CCY83928.1, ECO:0000313|Proteomes:UP000018054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1185 {ECO:0000313|Proteomes:UP000018054};
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 D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:CCY83928.1}.
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DR EMBL; CAYW010000195; CCY83928.1; -; Genomic_DNA.
DR AlphaFoldDB; R5LXJ2; -.
DR STRING; 1262921.BN473_00635; -.
DR Proteomes; UP000018054; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000018054}.
FT DOMAIN 19..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 137..246
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 297 AA; 32758 MW; E14502646BC1D7BA CRC64;
MRKFKKLVAI EPIKLTSEAK EKLKLYADEV IMHSDMPDTD SEITARIGDA DAVLVSFTTT
LTADILAKCS NLKYVGMCCS LYSPESANVD IRYAEGHGIT VTGIRDYGDE GVIEYVISEL
VRCLHGFGQP AWLGAPNEIT GLKAGIIGLG KSGGTIADAM KFFGAHIGYF ARSQKPEAEA
KGYRFMPLDK LVEWSDIVFC CLNRNTVLLH EKEFKLIGNH KILFNTGLSP AWDEPAMAQW
LDNDNICFCD TTGAAGSTNM QNHPHMHCMG VSSGLTKQSY ERLSNKVLTN IENYLKD
//
