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Database: UniProt
Entry: A0A0F5EVP6_AVIPA
LinkDB: A0A0F5EVP6_AVIPA
Original site: A0A0F5EVP6_AVIPA 
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
//
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