ID O84778_CHLTR Unreviewed; 346 AA.
AC O84778;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Leucine Dehydrogenase {ECO:0000313|EMBL:AAC68368.1};
GN Name=ldh {ECO:0000313|EMBL:AAC68368.1};
GN OrderedLocusNames=CT_773 {ECO:0000313|EMBL:AAC68368.1};
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561 {ECO:0000313|EMBL:AAC68368.1, ECO:0000313|Proteomes:UP000000431};
RN [1] {ECO:0000313|EMBL:AAC68368.1, ECO:0000313|Proteomes:UP000000431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx {ECO:0000313|Proteomes:UP000000431};
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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DR EMBL; AE001273; AAC68368.1; -; Genomic_DNA.
DR PIR; H71473; H71473.
DR RefSeq; NP_220292.1; NC_000117.1.
DR RefSeq; WP_009872153.1; NC_000117.1.
DR AlphaFoldDB; O84778; -.
DR STRING; 272561.CT_773; -.
DR EnsemblBacteria; AAC68368; AAC68368; CT_773.
DR GeneID; 884570; -.
DR KEGG; ctr:CT_773; -.
DR PATRIC; fig|272561.5.peg.849; -.
DR HOGENOM; CLU_025763_0_0_0; -.
DR InParanoid; O84778; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01075; NAD_bind_Leu_Phe_Val_DH; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR InterPro; IPR016211; Glu/Phe/Leu/Val/Trp_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42722; LEUCINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42722:SF1; VALINE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000188; Phe_leu_dh; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000188-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000188-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417};
KW Reference proteome {ECO:0000313|Proteomes:UP000000431}.
FT DOMAIN 145..345
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 83
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 180..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 346 AA; 37250 MW; 0150D491F492B64E CRC64;
MKYSLQIEDL HIEGYEQVLK VTCESVQLVA VIAIHQTKVG PALGGIRAFP YLQFEDGLQD
ALRLSKAMTY KALLSSTETG GGKSVIFLPK GMTSPTEGML RAFGQAVNSL QGKYIAAEDV
GVSVQDVMII REETPYVCGL VTVSGDPSIY TAHGVFLCIQ ETADYLCKTD IRGKRVAVQG
LGAVGRKLVH ELFFAGAELI VYDTRKDLLD EVVTLYGAQV DENIISADCD ILCPCALGGI
INSMSIDQLR CRAIVGATNN QLENPAIGRE LVARGILYAP DYLANAGGLL NVAGSVGRAY
SPKEVLSKVE GLPKILRKLY EQGAKENRDT GTLADAIVEE RLAVYA
//
