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Database: UniProt
Entry: D0J8J2_BLASP
LinkDB: D0J8J2_BLASP
Original site: D0J8J2_BLASP 
ID   D0J8J2_BLASP            Unreviewed;       309 AA.
AC   D0J8J2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00487};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_00487};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_00487,
GN   ECO:0000313|EMBL:ACX83663.1};
GN   OrderedLocusNames=BPLAN_024 {ECO:0000313|EMBL:ACX83663.1};
OS   Blattabacterium sp. subsp. Periplaneta americana (strain BPLAN)
OS   (Periplaneta americana symbiotic bacterium).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=600809 {ECO:0000313|EMBL:ACX83663.1, ECO:0000313|Proteomes:UP000002225};
RN   [1] {ECO:0000313|EMBL:ACX83663.1, ECO:0000313|Proteomes:UP000002225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPLAN {ECO:0000313|EMBL:ACX83663.1,
RC   ECO:0000313|Proteomes:UP000002225};
RX   PubMed=19880743; DOI=10.1073/pnas.0907504106;
RA   Sabree Z.L., Kambhampati S., Moran N.A.;
RT   "Nitrogen recycling and nutritional provisioning by Blattabacterium, the
RT   cockroach endosymbiont.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19521-19526(2009).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|HAMAP-Rule:MF_00487}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00487};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00487}.
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DR   EMBL; CP001429; ACX83663.1; -; Genomic_DNA.
DR   RefSeq; WP_012821192.1; NC_013418.2.
DR   AlphaFoldDB; D0J8J2; -.
DR   STRING; 600809.BPLAN_024; -.
DR   KEGG; bpi:BPLAN_024; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_10; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000002225; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01339; LDH-like_MDH; 1.
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   HAMAP; MF_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01763; MalateDH_bact; 1.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00487};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00487,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002225};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_00487}.
FT   DOMAIN          1..142
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          147..308
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         118..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   309 AA;  34105 MW;  F16838B378C38371 CRC64;
     MKVTIIGAGN VGASCASLLA EKDIVNEIVL LDIRDKFAEG KSLDISQMFP IIGSNTHIIG
     KTNDYSKSKN SEVIIITCGI PRKPGMSRDD LVNTNAKIIH SVTKESIHFS PKAKFIIVSN
     PLDVMSYVTY LTAKVDSSRV IGMAGILDSA RYRYFLSEEL NCSPHDIQTL LLGGHGDTMV
     PLYRYTSISG IPIMEFISKE KNQIIIEKTK KGGEQIINLL GTSAWMAPSA SVAQMVEAII
     KDSKRILSCS VFLKGEYDLK DVYLGVPVML GKSGIEKIIE LKLNQEEKNL LKKSANHVKN
     MIKKLENFH
//
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