GenomeNet

Database: UniProt
Entry: D5EQK3_CORAD
LinkDB: D5EQK3_CORAD
Original site: D5EQK3_CORAD 
ID   D5EQK3_CORAD            Unreviewed;       327 AA.
AC   D5EQK3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 91.
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=Caka_2804 {ECO:0000313|EMBL:ADE55817.1};
OS   Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 /
OS   KCTC 12865 / 04OKA010-24).
OC   Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC   Coraliomargaritaceae; Coraliomargarita.
OX   NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE55817.1, ECO:0000313|Proteomes:UP000000925};
RN   [1] {ECO:0000313|EMBL:ADE55817.1, ECO:0000313|Proteomes:UP000000925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865
RC   {ECO:0000313|Proteomes:UP000000925};
RX   PubMed=21304713; DOI=10.4056/sigs.952166;
RA   Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., Deshpande S.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Detter J.C., Woyke T.,
RA   Goodwin L., Pitluck S., Held B., Brettin T., Tapia R., Ivanova N.,
RA   Mikhailova N., Pati A., Liolios K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Coraliomargarita akajimensis type strain
RT   (04OKA010-24).";
RL   Stand. Genomic Sci. 2:290-299(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001998; ADE55817.1; -; Genomic_DNA.
DR   RefSeq; WP_013044539.1; NC_014008.1.
DR   AlphaFoldDB; D5EQK3; -.
DR   STRING; 583355.Caka_2804; -.
DR   KEGG; caa:Caka_2804; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_040727_2_0_0; -.
DR   OMA; TKGMERG; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000000925; 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:UP000000925};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN          7..151
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          157..325
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   327 AA;  34530 MW;  22C3E99C7228D954 CRC64;
     MSKEPIRVAV TGAAGNIGYA LLFRIASGAL FGPDQPVALN LIEIPPALDA LKGVVMELDD
     CAFPLLKDVV ATTDMDEGFK DVNWALLVGS VPRKAGMERG DLLGINGKVF TGQGKAIAAN
     AADDVRVVVV GNPCNTNCLI AMANAEGVPN DRFFAMTMLD ENRAKTQLAQ KAGVDVTEVT
     NMTIWGNHSA TQYPDFYSAK IGGKPANEVI GDDAWLKETF IPTVQKRGAA IIEARGASSA
     ASAANGAIDC VRKLTTDTPA GDSFSMCICS DGSYGTTPGL ITSLPCRVKD GKLEVVQGIE
     INEFSRAKID ASVKELEEEQ EAVKDLM
//
DBGET integrated database retrieval system