ID J6UAY0_9RHOB Unreviewed; 306 AA.
AC J6UAY0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:EJW09744.1};
GN ORFNames=A33M_0999 {ECO:0000313|EMBL:EJW09744.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW09744.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW09744.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW09744.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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:EJW09744.1}.
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DR EMBL; AKZI01000142; EJW09744.1; -; Genomic_DNA.
DR AlphaFoldDB; J6UAY0; -.
DR STRING; 1187851.A33M_0999; -.
DR PATRIC; fig|1187851.3.peg.4030; -.
DR eggNOG; COG0039; Bacteria.
DR Proteomes; UP000002930; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000002930}.
FT DOMAIN 2..137
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 140..298
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 113..115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 306 AA; 32527 MW; C7CE37990BF5BE1F CRC64;
MIGMGAVGTE VVAHLVASTV ASEIVAVDQN TAKAQAEMWD FAHTTSFIYA KNPRLVAGGY
ADTVGSDVVV ITAGAQLKQG ESRDVLVEVN TKVIRDIIAR VEATSPNAIV LMVTNPVDVM
AQVALTYSSF PKSRVIGLGT IVDTARFMRI VSEHVGIDPK NIFGWVLGDH SHTAFIPWSL
CNVCGLEVDT FCRLNGHAPL DRAAVRGRVL QIGLDIFAGK GNTNHGIAAS VFRIVRAIAG
NEHSVLPVGA MLEGEYGVEG AVMSVPCVIG RGGLQRIVAY RFDAEEQADF EASHAHVREL
LALAGL
//