ID V4IWK2_9GAMM Unreviewed; 331 AA.
AC V4IWK2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=D-lactate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N838_31050 {ECO:0000313|EMBL:ESQ14772.1};
OS Thiohalocapsa sp. PB-PSB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiohalocapsa.
OX NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ14772.1, ECO:0000313|Proteomes:UP000017935};
RN [1] {ECO:0000313|EMBL:ESQ14772.1, ECO:0000313|Proteomes:UP000017935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA Orphan V.J.;
RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT consortia of the Sippewissett salt marsh.";
RL Submitted (AUG-2013) 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:ESQ14772.1}.
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; AVFR01000551; ESQ14772.1; -; Genomic_DNA.
DR AlphaFoldDB; V4IWK2; -.
DR PATRIC; fig|1385625.5.peg.3707; -.
DR Proteomes; UP000017935; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000017935}.
FT DOMAIN 5..329
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..298
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 331 AA; 35693 MW; E5BA3339EB857471 CRC64;
MKIAFFHARG YERPSLEAEN TRHGHQISWF EATLAPETAA LAAGHDAVCI FVNDICNAEA
IATLADCGVR LILCRSAGYN QVDLAAARAH GLTVMRVPGY SPESVAEHTV GLILSLVRQL
HHQHNRVRDG NYALDGLVGF KLHQKTAGIF GTGRVGRAVA RILNGFGCRL LGYDIGENDE
MRALGMTYAS RETLLSESDI VILTLPLTPE THHLIDAESL ALIKPGAVLV NTGRGALVDT
RAAIDSLMAR DGLGYLGLDV YEEEAGKFFE DMSAQIVPDE TLLLLTNLRN ALVTPHSAFL
TRESLAEIAT ATLENATAFE AGQPDPDRVV A
//
