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Database: UniProt
Entry: I0LBS8_9ACTN
LinkDB: I0LBS8_9ACTN
Original site: I0LBS8_9ACTN 
ID   I0LBS8_9ACTN            Unreviewed;       316 AA.
AC   I0LBS8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:CCH21275.1};
DE            EC=1.1.1.37 {ECO:0000313|EMBL:CCH21275.1};
GN   Name=mdh {ECO:0000313|EMBL:CCH21275.1};
GN   ORFNames=MILUP08_46170 {ECO:0000313|EMBL:CCH21275.1};
OS   Micromonospora lupini str. Lupac 08.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH21275.1, ECO:0000313|Proteomes:UP000003448};
RN   [1] {ECO:0000313|Proteomes:UP000003448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX   PubMed=22815450; DOI=10.1128/jb.00628-12;
RA   Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA   Carro L., Coll P., Trujillo M.E.;
RT   "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT   Nodules of Lupinus angustifolius.";
RL   J. Bacteriol. 194:4135-4135(2012).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCH21275.1}.
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DR   EMBL; CAIE01000040; CCH21275.1; -; Genomic_DNA.
DR   RefSeq; WP_007464997.1; NZ_HF570108.1.
DR   AlphaFoldDB; I0LBS8; -.
DR   STRING; 1150864.MILUP08_46170; -.
DR   eggNOG; COG0039; Bacteria.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000003448; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd01339; LDH-like_MDH; 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; IPR011275; Malate_DH_type3.
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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW   ECO:0000313|EMBL:CCH21275.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003448};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          4..149
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          154..308
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         9..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         102
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         125..127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   316 AA;  32962 MW;  3A898FAE28B15E33 CRC64;
     MGKKVTVVGA GFYGSTTAQR LAEYDVFDTV VITDIVEGKP AGLALDLNQS RAIEGFETKV
     VGVTTGPNGE GYEAIEGSDV VVITAGLARK PGMSRMDLLE TNAKIVRQVA ENVAKYAPSA
     VVIVVSNPLD EMTALAQIAT QFPKNRVLGQ AGMLDTARFS NFVAEALNVP VASVRTLTLG
     SHGDTMVPVP SRSTVNGKPL RDAMPAEQIE ELVVKTRNGG AEVVALLKTG SAYYAPSAAA
     ARMAKAVAED SGDVMPVCAW VDGEYGISGV YLGVEAEIGA EGVRRVVETD LDADERASLL
     AAAEAVRAKQ GDVSSM
//
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