ID Q8EI78_SHEON Unreviewed; 329 AA.
AC Q8EI78;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 08-NOV-2023, entry version 120.
DE SubName: Full=Fermentative lactate dehydrogenase NADH dependent LdhA {ECO:0000313|EMBL:AAN54042.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:AAN54042.1};
GN Name=ldhA {ECO:0000313|EMBL:AAN54042.1};
GN OrderedLocusNames=SO_0968 {ECO:0000313|EMBL:AAN54042.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN54042.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN54042.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN54042.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54042.1; -; Genomic_DNA.
DR RefSeq; NP_716597.1; NC_004347.2.
DR RefSeq; WP_011071244.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EI78; -.
DR SMR; Q8EI78; -.
DR STRING; 211586.SO_0968; -.
DR PaxDb; 211586-SO_0968; -.
DR KEGG; son:SO_0968; -.
DR PATRIC; fig|211586.12.peg.929; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_6; -.
DR OMA; VIVTAHQ; -.
DR OrthoDB; 9805416at2; -.
DR PhylomeDB; Q8EI78; -.
DR BioCyc; SONE211586:G1GMP-902-MONOMER; -.
DR BRENDA; 1.1.1.28; 5706.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; 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|RuleBase:RU003719,
KW ECO:0000313|EMBL:AAN54042.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008186}.
FT DOMAIN 9..327
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; 36206 MW; A51E64A5FAD5BD7D CRC64;
MRIGFFSAKH YDMQHFNRTN AAFDAQIEYF DYRLCMQTVK LAEGFEVVCA FVNDSLCEEV
LVELAKGGTK IIAMRCAGFN NVDLVAAKRL GMQVVNVPAY SPESVAEHTV ALMLTLNRKI
HKAYQRTRDA NFSLEGLVGF NMFGKTVGVI GTGKIGVATI KVLLGFGCKV IAFDPYPNPA
VEALDVEYQD LDTIYATSDI ISLHCPLTPD NHHLLNKDSF AKMKPGVMVI NTSRGGLLNA
FDAMEALKLG QIGALGLDVY ENEKELFFED KSNQIIQDDV FRRLSACHNV IFTGHQAFLT
EEALGAIANT TLSNVQAVLA GKRCGNELF
//