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Database: UniProt
Entry: J6UAY0_9RHOB
LinkDB: J6UAY0_9RHOB
Original site: J6UAY0_9RHOB 
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
//
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