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Database: UniProt
Entry: A0A0A0B9H6_9CELL
LinkDB: A0A0A0B9H6_9CELL
Original site: A0A0A0B9H6_9CELL 
ID   A0A0A0B9H6_9CELL        Unreviewed;       362 AA.
AC   A0A0A0B9H6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:KGM03505.1};
GN   ORFNames=Q760_02445 {ECO:0000313|EMBL:KGM03505.1};
OS   Cellulomonas cellasea DSM 20118.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM03505.1, ECO:0000313|Proteomes:UP000029833};
RN   [1] {ECO:0000313|EMBL:KGM03505.1, ECO:0000313|Proteomes:UP000029833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM03505.1,
RC   ECO:0000313|Proteomes:UP000029833};
RA   Wang G., Zhuang W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:KGM03505.1}.
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DR   EMBL; AXNT01000012; KGM03505.1; -; Genomic_DNA.
DR   RefSeq; WP_034625295.1; NZ_AXNT01000012.1.
DR   AlphaFoldDB; A0A0A0B9H6; -.
DR   STRING; 1408250.Q760_02445; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000029833; Unassembled WGS sequence.
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; 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; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 2.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029833}.
FT   DOMAIN          2..140
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   ACT_SITE        182
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         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         103
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         127..129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         129
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   362 AA;  37841 MW;  27E10913C1A2D292 CRC64;
     MDVAVLGATG DVGRQVCTQL VERRVLPTSS RLQLVGRAGG SSARATHGLR ADLVDAYDEH
     APLIDVALAP EDVVADVVVV CAGVTAPPRA GASTDRTRLA AENHAVFDAY ARALAVHGSG
     NEVVVVVSNP VELGVAVMAR ALGRHRVIGM GAWLDTLRFR REIAVSLGLR RHRIGGFVAG
     QHGSDLVPLW STVRVSGLDR AERRRAIDAL RRGRTLATFG AEIADAQTRL LALAAEDIGA
     AFDLIDSWPP DLRAVARPWM THQSGAKTAA GTASATVDLV DTLLDGREIV VAGQVLLDGE
     VGVGGTALDG VLGVPVVLGP EGWTRALLDE PAPDEAELLV RCRDRIDASL APWGLGRAGV
     GA
//
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