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Database: UniProt
Entry: D7AXC5_NOCDD
LinkDB: D7AXC5_NOCDD
Original site: D7AXC5_NOCDD 
ID   D7AXC5_NOCDD            Unreviewed;       318 AA.
AC   D7AXC5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:ADH65999.1};
GN   OrderedLocusNames=Ndas_0552 {ECO:0000313|EMBL:ADH65999.1};
OS   Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS   7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS   (Actinomadura dassonvillei).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH65999.1, ECO:0000313|Proteomes:UP000002219};
RN   [1] {ECO:0000313|EMBL:ADH65999.1, ECO:0000313|Proteomes:UP000002219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC   NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC   {ECO:0000313|Proteomes:UP000002219};
RX   PubMed=21304737; DOI=10.4056/sigs.1363462;
RA   Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA   Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT   509).";
RL   Stand. Genomic Sci. 3:325-336(2010).
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DR   EMBL; CP002040; ADH65999.1; -; Genomic_DNA.
DR   RefSeq; WP_013151606.1; NC_014210.1.
DR   AlphaFoldDB; D7AXC5; -.
DR   STRING; 446468.Ndas_0552; -.
DR   KEGG; nda:Ndas_0552; -.
DR   eggNOG; COG0111; Bacteria.
DR   HOGENOM; CLU_019796_1_0_11; -.
DR   Proteomes; UP000002219; Chromosome 1.
DR   GO; GO:0051287; F:NAD binding; 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; 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; 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   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002219}.
FT   DOMAIN          107..281
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   318 AA;  34039 MW;  F49ADD5B70BB285A CRC64;
     MFVPERGRVL VSGRFEPDER ERIRTAAAGV PVDFVDGLGD RTDLLGTATV IAGTLSGEQL
     ALAPAVRWVH SWAAGVNNDL AAGLDAHPAV LTSSAGNGAV PLAEHAMMLM LMLNRDAPRW
     ARAQSERRWE RFQHGELNGL TCGIIGLGNC GLDLAAKARA FHMRVVGVRR RTDLPSPGVD
     AVHPPEDLHR MLAESDFVVV TAPDTPATEH LLGEAELRAM KDTAYVVVVS RGGIVADGAL
     LRALTEGWIA GAGLDAHGRE PLPPDSPFWD LPNVIVTPHN GATTAATRRR GVDVFVENLE
     RHARGRPLVN VVDKSAGY
//
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