ID A3D0X0_SHEB5 Unreviewed; 329 AA.
AC A3D0X0;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding {ECO:0000313|EMBL:ABN60383.1};
GN OrderedLocusNames=Sbal_0858 {ECO:0000313|EMBL:ABN60383.1};
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN60383.1, ECO:0000313|Proteomes:UP000001557};
RN [1] {ECO:0000313|EMBL:ABN60383.1, ECO:0000313|Proteomes:UP000001557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP000563; ABN60383.1; -; Genomic_DNA.
DR RefSeq; WP_006083996.1; NC_009052.1.
DR AlphaFoldDB; A3D0X0; -.
DR STRING; 325240.Sbal_0858; -.
DR GeneID; 11773660; -.
DR KEGG; sbl:Sbal_0858; -.
DR HOGENOM; CLU_019796_1_1_6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000001557; 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; cd12183; LDH_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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 9..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..297
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 329 AA; 36027 MW; 19C95656165100D1 CRC64;
MRIGFFSAKH YDMQHFNRTN AAFGAQIEYF DYRLCMQTVK LAEGFEIVCA FVNDSLCEEV
LVELAKGGTK IIAMRCAGFN NVDLVAAKRL GMQVVNVPAY SPESVAEHTV ALMLTLNRKI
HKAYQRTRDA NFSLEGLVGF NMFGKTVGVI GTGKIGVATI KVLLGFGCKV IAYDPFINPA
VVALNVEYQD LDAIYANSDI ISLHCPLTAD NRHLLNQASF AKMKPGVMVI NTSRGGLLNA
FDAMEALKLG QIGSLGLDVY ENEKGLFFED KSNEIIQDDV FRRLSACHNV IFTGHQAFLT
EEALGAIAQT TLSNVKALCA GERSGNELF
//
