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Database: UniProt
Entry: A0A0D2MXH8_9CHLO
LinkDB: A0A0D2MXH8_9CHLO
Original site: A0A0D2MXH8_9CHLO 
ID   A0A0D2MXH8_9CHLO        Unreviewed;       388 AA.
AC   A0A0D2MXH8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|RuleBase:RU003405};
DE            EC=1.1.1.37 {ECO:0000256|RuleBase:RU003405};
GN   ORFNames=MNEG_0778 {ECO:0000313|EMBL:KIZ07165.1};
OS   Monoraphidium neglectum.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX   NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ07165.1, ECO:0000313|Proteomes:UP000054498};
RN   [1] {ECO:0000313|EMBL:KIZ07165.1, ECO:0000313|Proteomes:UP000054498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ07165.1,
RC   ECO:0000313|Proteomes:UP000054498};
RX   PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA   Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA   Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA   Mussgnug J.H., Kruse O.;
RT   "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT   neglectum from its genome sequence reveals characteristics suitable for
RT   biofuel production.";
RL   BMC Genomics 14:926-926(2013).
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|RuleBase:RU003405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate;
CC         Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.82;
CC         Evidence={ECO:0000256|ARBA:ARBA00001500};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
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DR   EMBL; KK100287; KIZ07165.1; -; Genomic_DNA.
DR   RefSeq; XP_013906184.1; XM_014050730.1.
DR   AlphaFoldDB; A0A0D2MXH8; -.
DR   STRING; 145388.A0A0D2MXH8; -.
DR   GeneID; 25726896; -.
DR   KEGG; mng:MNEG_0778; -.
DR   OrthoDB; 312003at2759; -.
DR   Proteomes; UP000054498; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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   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; IPR011273; Malate_DH_NADP-dep_pln.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01757; Malate-DH_plant; 1.
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   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU003405};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN          44..191
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          194..363
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        225
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         167..169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   388 AA;  42055 MW;  1087B34AC5697C5B CRC64;
     MQTTTAPAAT EAAEGPAKYG VFRLAYDVAN EDPALTRNWK KTVHIAVTGA SGQISNHLLF
     MLASGEVFGR DQPVALQLLG SQRSREALEG VAMELEDSLY PLLREVSIGI DPREIFKGAD
     YALMVGAQPR GPGMERADLL DLNGRIFKDQ GQALNDVASP DVKVLVVGNP CNTNALIAME
     NAPRIPRKNF HALTRLDENR AKCQLALKSG KFYTNVNRVA IWGNHSTTQV PDFVNARIGG
     RPAIDVIGDM KWFRNEFTPT VAQRGGALIK KWGRSSAAST AVSVADAIRA LVTPTAPGDC
     FSSGVITDGN PYGIPDGLIF SMPCRSTGDG NYEICDDFII DDWLRSKINA SVDELVKEKE
     CVGHLIGTPN PVCRITKDDE DTWLPGEN
//
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