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Database: UniProt
Entry: A0A172ZGM8_9BACL
LinkDB: A0A172ZGM8_9BACL
Original site: A0A172ZGM8_9BACL 
ID   A0A172ZGM8_9BACL        Unreviewed;       314 AA.
AC   A0A172ZGM8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ORFNames=AR543_09875 {ECO:0000313|EMBL:ANF96280.1};
OS   Paenibacillus bovis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF96280.1, ECO:0000313|Proteomes:UP000078148};
RN   [1] {ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA   Wu Z., Gao C., Liu Z., Zheng H.;
RT   "Genome of Paenibacillus bovis sp. nov.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANF96280.1, ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|EMBL:ANF96280.1,
RC   ECO:0000313|Proteomes:UP000078148};
RX   PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA   Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT   "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT   milk.";
RL   Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
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; CP013023; ANF96280.1; -; Genomic_DNA.
DR   RefSeq; WP_060533996.1; NZ_CP013023.1.
DR   AlphaFoldDB; A0A172ZGM8; -.
DR   STRING; 1616788.AR543_09875; -.
DR   KEGG; pbv:AR543_09875; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000078148; 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.
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:UP000078148};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_00487}.
FT   DOMAIN          8..148
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          153..310
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         13..18
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         37
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         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         101
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         124..126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   314 AA;  33493 MW;  227C60CE326FE33E CRC64;
     MTAIKRKKIT VVGAGFTGAT TALMLAQKEL GDVVLVDIPQ LENPTKGKAL DMMEASPVQG
     FDSQIKGTSD YNDTKDSDVV IITAGVARKP GMSRDDLVNT NAGIVRSVCE QVKQQAPESI
     VIILSNPVDA MTHVAYQALG FPKTRVIGQS GVLDTARYCT FIAEELNVSV EDVRGFVLGG
     HGDDMVPLVR YSSVGGIPID TLISSERIEA IVQRTRVGGG EIVNLLGNGS AYYAPAASLV
     QMTEAVLKDK KRILPVIAYL EGEYGYENLF MGIPAILGGD GIEKIFELEL TSDEKAALDK
     SAESVRSVIK VITG
//
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