ID C7Q074_CATAD Unreviewed; 370 AA.
AC C7Q074;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:ACU75567.1};
GN OrderedLocusNames=Caci_6721 {ECO:0000313|EMBL:ACU75567.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU75567.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU75567.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001700; ACU75567.1; -; Genomic_DNA.
DR AlphaFoldDB; C7Q074; -.
DR STRING; 479433.Caci_6721; -.
DR KEGG; cai:Caci_6721; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_11; -.
DR InParanoid; C7Q074; -.
DR Proteomes; UP000000851; Chromosome.
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; cd12167; 2-Hacid_dh_8; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT DOMAIN 80..176
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 177..330
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 370 AA; 38784 MW; 00D4838BC2833630 CRC64;
MYHPHRHTAE GEIILTTSHT AASVPAPATA PDRPTLLLAV TAEESALVLD AESHQRLAAT
AGLVSGGPLP SLGEPAFTAA LAGTEILLTS WSSPRIDAEL LAAAPRLRLV VHAAGTVKFL
MAPEAFAAGV RVCSAAEANA VPVAEYTLAA IILGAKRAFT AAARYRRGLR SADGTHRNLD
GISPIGTHRM TVGVVGASRI GRKVVRLLRD VLDADVLIYD PYGAGDLTAD PRVRLTSLEE
LLAASEVVSL HAPLTPLTRG MLDARGLALM RDGAVLVNTA RGGIVDQTAL TAELVSGRID
AVLDVTATEP LPPDSVLFTL PNVFLTPHIA GALGGEVLRL GRLAVEEVER YVAGLPLRYE
VLPDQLERLA
//
