ID F7NEN6_9FIRM Unreviewed; 316 AA.
AC F7NEN6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:EGO65447.1};
GN ORFNames=ALO_02506 {ECO:0000313|EMBL:EGO65447.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO65447.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO65447.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO65447.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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:EGO65447.1}.
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DR EMBL; AFGF01000017; EGO65447.1; -; Genomic_DNA.
DR RefSeq; WP_004092485.1; NZ_AFGF01000017.1.
DR AlphaFoldDB; F7NEN6; -.
DR STRING; 1009370.ALO_02506; -.
DR eggNOG; COG0111; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000003240; 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 CDD; cd05300; 2-Hacid_dh_1; 1.
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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240}.
FT DOMAIN 37..310
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..279
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 316 AA; 35562 MW; D05BB8B51367FC90 CRC64;
MPALNVLFLN PLAERHTQTI TNMIPDTSVI SCDLAHAPEY IENTDILVAW GFADIRRLYL
AAPKLKWVHA LSAGVENLVF PEIQQSNTIL TNSRGIHGIP VSEHVFAFML AFTRGFNLFI
RQQQQHIWKR VEPQEIHEKT IGIVGLGSIG REIAKRAKGL GMHVLATKRT ATTEIFVDKM
YPAERMNEML SQCDFVVVTL PLTEDTKGLF RLEQFSAMKR TAYFINIARG AVVCQPDLAD
ALEQGLIQGA GLDVFEHEPL PAESPLWDMS NVIITPHVAA LSPHYLDRAV KLFADNLLRY
VNDREMFNVI DKVKGY
//
