ID B4D576_9BACT Unreviewed; 328 AA.
AC B4D576;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:EDY18281.1};
GN ORFNames=CfE428DRAFT_4065 {ECO:0000313|EMBL:EDY18281.1};
OS Chthoniobacter flavus Ellin428.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY18281.1, ECO:0000313|Proteomes:UP000005824};
RN [1] {ECO:0000313|EMBL:EDY18281.1, ECO:0000313|Proteomes:UP000005824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY18281.1,
RC ECO:0000313|Proteomes:UP000005824};
RX PubMed=21460085; DOI=10.1128/JB.00295-11;
RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA Smidt H.;
RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT heterotrophic soil bacterium.";
RL J. Bacteriol. 193:2902-2903(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:EDY18281.1}.
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DR EMBL; ABVL01000013; EDY18281.1; -; Genomic_DNA.
DR RefSeq; WP_006981389.1; NZ_ABVL01000013.1.
DR AlphaFoldDB; B4D576; -.
DR STRING; 497964.CfE428DRAFT_4065; -.
DR GeneID; 78183613; -.
DR eggNOG; COG1052; Bacteria.
DR InParanoid; B4D576; -.
DR Proteomes; UP000005824; 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 GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR CDD; cd05299; CtBP_dh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR043322; CtBP.
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; PTHR46029; C-TERMINAL-BINDING PROTEIN; 1.
DR PANTHER; PTHR46029:SF7; C-TERMINAL-BINDING 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 Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000005824}.
FT DOMAIN 29..325
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 117..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 35333 MW; A86C1072A5E203AB CRC64;
MSSPKPLIGI IDWAKSPLGE PECTAERAVI GDAAEVRRFL CSSDDDFTDE ICGADALIVW
HNTPIRAAGL ARLRQCRALI RNGVGFDSVD IAAAREHGIA VCNVPDYGTE EVADHAIALA
LALCRQLFPL DREAKQLGWT IRVEPRLRRL RELTFGVVGL GRIGTAAALR AKALGFKVVF
YDPYLPNGVD KAVGIVRVRQ LDELLRQADV VSLHCPLTEE TRHLIAEREI ALLKPGAFVV
NTARGAVIKK TAILDALRTG RIAGAGLDVV EDEPLQTAEE AATPNLIVTC HAAFCSVESK
LEMRATSARI ALAAVRGEPL ENIVNGVG
//
