ID A0A0F5EVP6_AVIPA Unreviewed; 316 AA.
AC A0A0F5EVP6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=L-lactate dehydrogenase {ECO:0000313|EMBL:SUU98489.1};
DE EC=1.1.1.27 {ECO:0000313|EMBL:SUU98489.1};
GN Name=ldh {ECO:0000313|EMBL:SUU98489.1};
GN ORFNames=NCTC10926_01922 {ECO:0000313|EMBL:SUU98489.1};
OS Avibacterium paragallinarum (Haemophilus gallinarum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Avibacterium.
OX NCBI_TaxID=728 {ECO:0000313|EMBL:SUU98489.1, ECO:0000313|Proteomes:UP000254620};
RN [1] {ECO:0000313|EMBL:SUU98489.1, ECO:0000313|Proteomes:UP000254620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10926 {ECO:0000313|EMBL:SUU98489.1,
RC ECO:0000313|Proteomes:UP000254620};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|RuleBase:RU003369}.
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DR EMBL; UFSW01000001; SUU98489.1; -; Genomic_DNA.
DR RefSeq; WP_046098882.1; NZ_VXDA01000008.1.
DR AlphaFoldDB; A0A0F5EVP6; -.
DR STRING; 728.VY92_06335; -.
DR eggNOG; COG0039; Bacteria.
DR OMA; CYIIVLT; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000254620; Unassembled WGS sequence.
DR GO; GO:0004459; F:L-lactate 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 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,
KW ECO:0000313|EMBL:SUU98489.1}.
FT DOMAIN 1..140
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 147..310
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 316 AA; 34706 MW; 2B85CB30605FACA8 CRC64;
MKVSIIGAGA VGVGICNYLL TMGECQEVVL VDLNKERTRG EQLDFSHTSA LTFAKNTKII
SGEYEDTRDS DVVVITAGAQ IKVGQDRLEI GHINAKITVE IARQLERYTP NAIIIVVTNP
CDILTHFIIR NTNFPAHRVI SAGCVVDTAR MMKIIADKVK IDPKNVFGYM MGEHGANSFI
PWSIVNIAGQ KIDDFCQQND VPMLDPQELL KATKAIGLEV FSLKLNTNHA IAASVFRIIR
AISINEYSVL PVGTMLNGEY GLNDVVVNVP MVISSKGVER ILKYKLPADE LEQLHQCAKA
LRQVVEQVAE STGLKC
//