ID A0A0J9H0Q4_9RHOB Unreviewed; 392 AA.
AC A0A0J9H0Q4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KMW59318.1};
DE EC=1.1.1.37 {ECO:0000313|EMBL:KMW59318.1};
GN ORFNames=AIOL_004300 {ECO:0000313|EMBL:KMW59318.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW59318.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW59318.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW59318.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KMW59318.1}.
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DR EMBL; LFTY01000002; KMW59318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9H0Q4; -.
DR STRING; 1675527.AIOL_004300; -.
DR PATRIC; fig|1675527.3.peg.4500; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000037178; Unassembled WGS sequence.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
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:SF34; L-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 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 Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW ECO:0000313|EMBL:KMW59318.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037178}.
FT DOMAIN 90..229
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 233..390
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
SQ SEQUENCE 392 AA; 40863 MW; 6D1AFF34040FA6E5 CRC64;
MSRVVGSELI EDARQRGRVV FEILPGDIIT DVARETAARI GIRLVDGPLE RPAPVKTDGT
TAMRRLMYKR SARWVAPRRG AILPARRFSK LALVGAGGVG GNIAHLAAMA DMADEIALID
IAPGLAAATA LDLNHATGIT GARARCLGGE DLSQVSGADV VVVTAGRARS PGMTRADLIG
VNARVIQTAA EAIRTQAPQA IVIVVTNPLD EMTTEMLRAT GFPRERVLGM AGTLDSSRFR
NALAMAAGVT PADVQAITLG SHGEEMAPIP SLARIKGAPL EKFLSPERIA ACVQDAVTGG
GQVVALKKMG SATIAPAHAS VELLDHIRGA RSGPVPVSVR LDGEYGIEGV VLGVPAHLGA
SGLVEVEELR LTEEERDALR RAADAIKARL AS
//
