ID D1LBB6_9NEOP Unreviewed; 141 AA.
AC D1LBB6;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|RuleBase:RU003405};
DE EC=1.1.1.37 {ECO:0000256|RuleBase:RU003405};
DE Flags: Fragment;
GN Name=MDH {ECO:0000313|EMBL:ACZ27442.1};
OS Cyllogenes woolletti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Satyrinae; Melanitini; Cyllogenes.
OX NCBI_TaxID=681781 {ECO:0000313|EMBL:ACZ27442.1};
RN [1] {ECO:0000313|EMBL:ACZ27442.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19793750; DOI=10.1098/rspb.2009.1303;
RA Wahlberg N., Leneveu J., Kodandaramaiah U., Pena C., Nylin S.,
RA Freitas A.V., Brower A.V.;
RT "Nymphalid butterflies diversify following near demise at the
RT Cretaceous/Tertiary boundary.";
RL Proc. R. Soc. B 276:4295-4302(2009).
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 -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000256|ARBA:ARBA00009613}.
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DR EMBL; GQ865195; ACZ27442.1; -; Genomic_DNA.
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; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF3; MALATE DEHYDROGENASE, CYTOPLASMIC; 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 3: Inferred from homology;
KW NAD {ECO:0000256|RuleBase:RU003405};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}.
FT DOMAIN 1..103
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 107..140
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACZ27442.1"
FT NON_TER 141
FT /evidence="ECO:0000313|EMBL:ACZ27442.1"
SQ SEQUENCE 141 AA; 15246 MW; FB50C6BBDDBF631F CRC64;
LEGVVMELAD CALPLLAXVL PTANPEEAFK DVAAAFLVGA MPRREGMERK DLLSANVRIF
KEQGQALDKV ARKDVKVLVV GNPANTNALI CSKYAPSIPK ENFTAMTRLD QNRAQSQLAA
KIGVPVQDVK NVIIWGNHSS P
//