ID Q1ZM03_PHOAS Unreviewed; 317 AA.
AC Q1ZM03;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:EAS63250.1};
DE EC=1.1.1.272 {ECO:0000313|EMBL:EAS63250.1};
GN ORFNames=VAS14_08225 {ECO:0000313|EMBL:EAS63250.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS63250.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS63250.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS63250.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:EAS63250.1}.
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DR EMBL; AAOJ01000009; EAS63250.1; -; Genomic_DNA.
DR RefSeq; WP_005369882.1; NZ_CH902600.1.
DR AlphaFoldDB; Q1ZM03; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000001603; Unassembled WGS sequence.
DR GO; GO:0050578; F:(R)-2-hydroxyacid dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12162; 2-Hacid_dh_4; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; 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 25..314
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 34835 MW; BB97338EA943D10F CRC64;
MEHIVFLDRA TIPAHIDIPR PQSDHQWVEY QRTLPSQVIE RLQHATIAIS NKVQLTADIL
SQLPNLKFIA IGATGTNNVD LDYCHRHNIP VSNIRGYATR SVPEHVLAMI FALKRNLIGY
QQDIIAGEWQ KQQQFCFFTH PISDIAGSTM GVIGKGSLGV ATANLANALG MKILFAEHKH
VPTCREGYTL FNDVLQQADI ITLHCPLTDT TEDLIAKTEL AQMKPNAILI NTGRGGLVNE
QDLVDALLAK KIAGAGCDVF TSEPPTDDNP LLQQAHLPNL LLTPHVAWGS DSAITALVNQ
LIENIECFCN GKPHNLV
//
