ID F6EKX2_HOYSD Unreviewed; 326 AA.
AC F6EKX2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:AEF41452.1};
GN OrderedLocusNames=AS9A_3005 {ECO:0000313|EMBL:AEF41452.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF41452.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF41452.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002786; AEF41452.1; -; Genomic_DNA.
DR RefSeq; WP_013807801.1; NC_015564.1.
DR AlphaFoldDB; F6EKX2; -.
DR STRING; 443218.AS9A_3005; -.
DR KEGG; asd:AS9A_3005; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_11; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000009235; 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; 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:UP000009235}.
FT DOMAIN 36..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 35215 MW; 37266D05B2F84704 CRC64;
MTTAAERTRP IVAVLYREAL PPRLAEIEEL SDVRLTTADG LAKALDGADV LYQWHSFSPA
LRENWDAAAS LRWVHVSAAG VSQLLFDELI RSDIAYTNSR GVLSRAIAEF ALGFVLDMAK
DAQTSFRLQQ QHRWRHRTTR KLQGQSALVV GTGSIGREIA RLFEAVGIEV SGAGRSSRSG
DGDFRQIHSS RDLASVVRDY DYLVLAAPLT PETRGLVSAQ VLASMKPTAS LINVGRGELV
DTDALTGALA SAGIAGAALD VVHPEPLPEG HALWGMDNVI ITPHMSGDTD DYLDDLGQLF
VDNLRRYCNG APLQNVVDKA LGFVSA
//
