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Database: UniProt
Entry: C6WLQ8_ACTMD
LinkDB: C6WLQ8_ACTMD
Original site: C6WLQ8_ACTMD 
ID   C6WLQ8_ACTMD            Unreviewed;       329 AA.
AC   C6WLQ8;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   OrderedLocusNames=Amir_6492 {ECO:0000313|EMBL:ACU40293.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS   / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU40293.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU40293.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC   NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA   Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|HAMAP-Rule:MF_01517}.
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_01517,
CC         ECO:0000256|RuleBase:RU000422};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613, ECO:0000256|HAMAP-Rule:MF_01517}.
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DR   EMBL; CP001630; ACU40293.1; -; Genomic_DNA.
DR   RefSeq; WP_015805176.1; NC_013093.1.
DR   AlphaFoldDB; C6WLQ8; -.
DR   STRING; 446462.Amir_6492; -.
DR   KEGG; ami:Amir_6492; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_040727_2_0_11; -.
DR   OMA; TKGMERG; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01338; MDH_choloroplast_like; 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_01517; Malate_dehydrog_2; 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; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 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.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN          7..148
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          157..324
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         12..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         106
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517"
FT   BINDING         130..132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   329 AA;  34646 MW;  E9959BA470E91866 CRC64;
     MTRTPVNVTV TGAAGQIGYA LLFRIASGHL LGPDVPVRLR LLEIPQAVKA AEGTAMELDD
     CAFPLLDGID ITDDATKAFD GVNVALLVGA RPRTKGMERG DLLQANGGIF KPQGEAINAG
     AADDVRVLVV GNPANTNALI AQQHAPDVPA ERFTAMTRLD HNRALSQLAK KLGVSVDDIK
     KLTIWGNHSA TQYPDLFNAE VAGKNAAEAV NDQAWLENDF IPTVAKRGAA IIEARGASSA
     ASAANAALNH IHDWVNGTAE GDWVSMAIPS DGSYGVPEGL ISSFPVTVKD GKYSIVQGLE
     INEFSRARID ASVAELVEER DAVKALGLI
//
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