ID D6QT55_9LECA Unreviewed; 231 AA.
AC D6QT55;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
DE Flags: Fragment;
OS Rhizoplaca chrysoleuca.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Lecanoraceae;
OC Rhizoplaca.
OX NCBI_TaxID=112062 {ECO:0000313|EMBL:ADG23098.1};
RN [1] {ECO:0000313|EMBL:ADG23098.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20953937;
RA Wang H., Guo S., Huang M., Thorsten L.H., Wei J.;
RT "Ascomycota has a faster evolutionary rate and higher species diversity
RT than Basidiomycota.";
RL Sci. China Life Sci. 53:1163-1169(2010).
RN [2] {ECO:0000313|EMBL:ADG23098.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang H.Y., Thorsten L.H., Guo S.Y., Huang M.R., Wei J.C.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824}.
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DR EMBL; HM007281; ADG23098.1; -; mRNA.
DR AlphaFoldDB; D6QT55; -.
DR GO; GO:0030060; F:L-malate dehydrogenase 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 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; 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; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11540:SF73; MALATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 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 2: Evidence at transcript level;
KW NAD {ECO:0000256|RuleBase:RU003405};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU003405}.
FT DOMAIN 25..168
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 170..223
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT NON_TER 231
FT /evidence="ECO:0000313|EMBL:ADG23098.1"
SQ SEQUENCE 231 AA; 24023 MW; E32DE7836871A0BB CRC64;
MRASRQLFGA CQRRAFSASA RQASKVTVLG GAGGIGQPLS LLMKLNPRVT ELAIYDIKGG
PGVAADIGHI NTKSTVTGYQ PDANGLKEAL TGSEIVLIPA GVPRKPGMTR DDLFNTNASI
VRDLAKAVAS SAPEANVLVI SNPVNSTVPI CAEIFKGAGV YNPKRLFGVT TLDVVRASRF
ISQHKNTDPA DENITVVGGH SGATIVPAVS QSGYELQGRS SMIHIQGAYG G
//
