ID A0A077FLA0_9RICK Unreviewed; 325 AA.
AC A0A077FLA0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:AIL64834.1};
DE EC=1.1.1.37 {ECO:0000313|EMBL:AIL64834.1};
GN Name=mdh_1 {ECO:0000313|EMBL:AIL64834.1};
GN ORFNames=NOVO_02195 {ECO:0000313|EMBL:AIL64834.1};
OS Rickettsiales bacterium Ac37b.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=1528098 {ECO:0000313|EMBL:AIL64834.1, ECO:0000313|Proteomes:UP000028936};
RN [1] {ECO:0000313|EMBL:AIL64834.1, ECO:0000313|Proteomes:UP000028936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac37b {ECO:0000313|EMBL:AIL64834.1,
RC ECO:0000313|Proteomes:UP000028936};
RA Felsheim R.F., Kurtti T.J., Johnson S., Labruna M.B., Munderloh U.G.;
RT "Genome sequence of a novel Rickettsiales species cultured from Amblyomma
RT cajennense.";
RL Submitted (JAN-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}.
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DR EMBL; CP009217; AIL64834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077FLA0; -.
DR STRING; 1528098.NOVO_02195; -.
DR KEGG; rbt:NOVO_02195; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_2_5; -.
DR OrthoDB; 9771883at2; -.
DR Proteomes; UP000028936; Chromosome.
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 PIRSF; PIRSF000102; Lac_mal_DH; 1.
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|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW ECO:0000313|EMBL:AIL64834.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028936}.
FT DOMAIN 5..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 164..320
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 127..129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 325 AA; 36181 MW; 7E3AD34C83B77B66 CRC64;
MDRKRIGIIG AGDIGLNLAE IMALQGYDVV VFNRYHAVDN KPSPYWLSKM GTIMDMNDSL
QLPNCGEVSL TSDLSDLSNV NIIVITAGAK RTNTAETREE LAGKNARIMD NYINIIAENP
NTLILIISNP VDFLTQYLIN KISEVSGQTK DKIAQRIIGV SYIDTMRLQN LIREFLKTSY
PSIIKPKINA IVLGEHGPSM VPITSNVTIN GKLLSELASL EQIDYITSHT ILRGNDIIKL
TGASSVVGPS HAVMHMITNI LNDKEALLPC SIWDGKRSIG KLAKFVDRYF TDIIEINISN
DEKEKLHISE QTLDTQYKKI MTYLE
//
