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Database: UniProt
Entry: G2GP30_9ACTN
LinkDB: G2GP30_9ACTN
Original site: G2GP30_9ACTN 
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}.
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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
//
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