ID A0A094LQL7_9GAMM Unreviewed; 331 AA.
AC A0A094LQL7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:KFZ37468.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:KFZ37468.1};
GN ORFNames=HR45_10660 {ECO:0000313|EMBL:KFZ37468.1};
OS Shewanella mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1515746 {ECO:0000313|EMBL:KFZ37468.1, ECO:0000313|Proteomes:UP000029264};
RN [1] {ECO:0000313|EMBL:KFZ37468.1, ECO:0000313|Proteomes:UP000029264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YQH10 {ECO:0000313|EMBL:KFZ37468.1,
RC ECO:0000313|Proteomes:UP000029264};
RA Liu Y., Zeng R.;
RT "Shewanella sp. YQH10.";
RL Submitted (JUN-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ37468.1}.
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DR EMBL; JPEO01000006; KFZ37468.1; -; Genomic_DNA.
DR RefSeq; WP_037442647.1; NZ_JPEO01000006.1.
DR AlphaFoldDB; A0A094LQL7; -.
DR STRING; 1515746.HR45_10660; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000029264; Unassembled WGS sequence.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000029264}.
FT DOMAIN 9..329
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..299
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 331 AA; 36552 MW; DC6CB1235C4DE81B CRC64;
MKIGFFSAKR YDIQHFSKTN EAGNFGADIE FFDYRLSRQN VRLALGFEVI CAFVNDELCE
EVLTKLYASG TKIIAMRCAG FNNVDLDAAK RLGLEVVNVP AYSPESVAEH TVALMLTLNR
KIHKSYGRTR DANFSLEGLV GFNMHGKTVG VIGTGKIGIA TIRILRGFGC EVLAYDPFHN
PLAEELGASY ASLDDIYQNS DIISLHCPLT KDNQHLLNAE SFAKMKPGMM VINTSRGGLL
NAVDAMEALK MGQIGSLGLD VYENEKELFF EDKSNEVILD DVFRRLSACH NVIFTGHQAF
LTREALDNIA QTTLSNVSQI LAGKKCGNEL F
//
