ID D3HMC7_LEGLN Unreviewed; 311 AA.
AC D3HMC7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Putative D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:CBJ13616.1};
GN OrderedLocusNames=LLO_3163 {ECO:0000313|EMBL:CBJ13616.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ13616.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ13616.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ13616.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FN650140; CBJ13616.1; -; Genomic_DNA.
DR RefSeq; WP_003634460.1; NC_013861.1.
DR AlphaFoldDB; D3HMC7; -.
DR STRING; 661367.LLO_3163; -.
DR KEGG; llo:LLO_3163; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000001060; 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; cd12172; PGDH_like_2; 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001060}.
FT DOMAIN 36..309
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 311 AA; 34011 MW; 512E68890C83C1C4 CRC64;
MKVLVTCPPM LGLIDHFYQH ALNSGIELVP AKTVQVLSVR ELLELVPQYD GWIIGDDPAT
REVFTAGTKG RLKAAVKWGI GVDNVDFKAC HDLNIPITNT PNMFGGEVAD VAIAYLLGLA
RHLFYIDREV RNNNWAKPAG MSMAGKHIGV IGFGDIGENI VKRLAGFDVK VTVYDPFIEG
DKGYNFVHRK NFPEGLSELD FLILACALTK QNIHLLNAKT ISLLKEGAKI INVSRGLLIH
EQALIDALNS GHISSAALEV FEEEPLPQNS PLRALPQCIL GSHNASNTVE GVKRASMEAI
KKIAEFLNAK Q
//
