ID G2GP30_9ACTN Unreviewed; 333 AA.
AC G2GP30;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:EGX54734.1};
GN ORFNames=SZN_36429 {ECO:0000313|EMBL:EGX54734.1};
OS Streptomyces zinciresistens K42.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX54734.1, ECO:0000313|Proteomes:UP000004217};
RN [1] {ECO:0000313|EMBL:EGX54734.1, ECO:0000313|Proteomes:UP000004217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K42 {ECO:0000313|EMBL:EGX54734.1,
RC ECO:0000313|Proteomes:UP000004217};
RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EGX54734.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGBF01000337; EGX54734.1; -; Genomic_DNA.
DR AlphaFoldDB; G2GP30; -.
DR PATRIC; fig|700597.3.peg.7077; -.
DR Proteomes; UP000004217; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000004217}.
FT DOMAIN 9..142
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 149..200
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT REGION 308..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 13..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 123..125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 333 AA; 34718 MW; E0FA14A6223A4E48 CRC64;
MTPPPLEAVG VIGAGAVGQA VSTALVASAP PGRLLIASRV LDQAVALAAD LGDMRHATAS
PVHPEACDVE GLADCTAVVV AVRTAFTNTH TADVRMAGAA ANAPVIRALA ACLHGYQGTV
LVVTNPVDLM PRLFAEASGC PRVYGIGSNL DSARFRLTLA RLLNVPADAV QGHVIGEHGD
GAVVCASSTT VNGTPAQVPL AEVRAELRTR PGRISAGVGR TRSGPAGAVL SALRKALGLV
DGTEELTAEH RGDWLGIPLR FTSGRPVACL PALNADEDAQ LAATLTKLRG AYGRSAVLPH
PQPLWRRREY PYRHPAAGRG RERDRAQQHR LRH
//