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Database: UniProt
Entry: A0A0D5ABR8_9NOCA
LinkDB: A0A0D5ABR8_9NOCA
Original site: A0A0D5ABR8_9NOCA 
ID   A0A0D5ABR8_9NOCA        Unreviewed;       307 AA.
AC   A0A0D5ABR8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:AJW40281.1};
GN   ORFNames=NY08_2253 {ECO:0000313|EMBL:AJW40281.1};
OS   Rhodococcus sp. B7740.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW40281.1, ECO:0000313|Proteomes:UP000032410};
RN   [1] {ECO:0000313|EMBL:AJW40281.1, ECO:0000313|Proteomes:UP000032410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7740 {ECO:0000313|EMBL:AJW40281.1};
RX   PubMed=25931596;
RA   Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT   "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT   Bacterium Isolated from the Arctic Sea.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CP010797; AJW40281.1; -; Genomic_DNA.
DR   RefSeq; WP_045196323.1; NZ_CP010797.1.
DR   AlphaFoldDB; A0A0D5ABR8; -.
DR   STRING; 1564114.NY08_2253; -.
DR   KEGG; rhb:NY08_2253; -.
DR   PATRIC; fig|1564114.4.peg.2214; -.
DR   HOGENOM; CLU_045401_2_2_11; -.
DR   Proteomes; UP000032410; Chromosome.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT   DOMAIN          5..143
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          148..291
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         10..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   307 AA;  32351 MW;  EE33E009DEF779C8 CRC64;
     MNTNKVTIFG GAGGIGSSVA FNLLLRPPTY DVVIVDTKPN MVTSHVMDLQ DVAGVDGSST
     VRGGSADDAA DSDIVILSAA VPLRLNASRS VFLEDNARIV DTLAVPLIES GWNGILIMLT
     NPADALITWL HQRTGYDRRK LLGYTINDSL RLRTGVGRAL GVSPHRVEGW VLGEHGAGQV
     PLYDSLLLDG SPVHLDDEQR AVAQNYIDTW YVEHVALDSG RTSTWSSGRG TALLVDAIVT
     ESDEPLPASV VLDGEYGVKG AGLGVPVLLG RSGVRSIAEW DLSPSDLAAF RAGGDSVLAA
     ADSISQV
//
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