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Database: UniProt
Entry: D5VSV9_METIM
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ID   D5VSV9_METIM            Unreviewed;       312 AA.
AC   D5VSV9;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Malate dehydrogenase (NADP(+)) {ECO:0000313|EMBL:ADG13662.1};
DE            EC=1.1.1.82 {ECO:0000313|EMBL:ADG13662.1};
GN   OrderedLocusNames=Metin_1004 {ECO:0000313|EMBL:ADG13662.1};
OS   Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG13662.1, ECO:0000313|Proteomes:UP000002061};
RN   [1] {ECO:0000313|EMBL:ADG13662.1, ECO:0000313|Proteomes:UP000002061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanocaldococcus infernus ME.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|ARBA:ARBA00008104, ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CP002009; ADG13662.1; -; Genomic_DNA.
DR   RefSeq; WP_013100407.1; NC_014122.1.
DR   AlphaFoldDB; D5VSV9; -.
DR   SMR; D5VSV9; -.
DR   STRING; 573063.Metin_1004; -.
DR   GeneID; 9132020; -.
DR   KEGG; mif:Metin_1004; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_2_2_2; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 2596at2157; -.
DR   Proteomes; UP000002061; Chromosome.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR018177; L-lactate_DH_AS.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369}.
FT   DOMAIN          1..145
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          148..311
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         7..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         121..123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   312 AA;  34467 MW;  3840534D8290D84D CRC64;
     MKVSIIGASG KVGSAISFLL ANEPYVKELV LISREKSIDK LRGLREDIYD ALAGTKRDCE
     INVSDDKTLK FLDGSDLVII TSGVPRTPEM SRLDLAKVNA KIIGNYAKKI AEICETKLFI
     ITNPVDVMTY KAYIDSKFER NKVFGLGTHL DSLRFKVEIA KFFGVHIDEV RTRIIGEHGD
     TMVPLISSTS IGGIPITRFK SFKDLPLKDI IENVKNKGSK IIALKGGSEF GPAAAVLNVV
     RSIANNENRL LTLSTYLDGE FGFSDVCAGV PVKVGKDGVE IVTDIVFSKE EFEAFKYSIE
     TIKRYCEEIK EL
//
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