ID A4HWJ9_LEIIN Unreviewed; 1020 AA.
AC A4HWJ9; A0A2K4YQG7; A0A381MED0;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN Name=GDH {ECO:0000313|EMBL:CAM66827.2};
GN ORFNames=LINJ_15_1070 {ECO:0000313|EMBL:CAM66827.2};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM66827.2, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAM66827.2, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM66827.2,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM66827.2, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM66827.2,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
CC -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC glutamate to ammonia and alpha-ketoglutarate.
CC {ECO:0000256|PIRNR:PIRNR000184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC Evidence={ECO:0000256|PIRNR:PIRNR000184};
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000184}.
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; FR796447; CAM66827.2; -; Genomic_DNA.
DR RefSeq; XP_001464440.2; XM_001464403.2.
DR AlphaFoldDB; A4HWJ9; -.
DR SMR; A4HWJ9; -.
DR STRING; 5671.A4HWJ9; -.
DR GeneID; 5067833; -.
DR KEGG; lif:LINJ_15_1070; -.
DR VEuPathDB; TriTrypDB:LINF_150018300; -.
DR eggNOG; KOG2250; Eukaryota.
DR InParanoid; A4HWJ9; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000008153; Chromosome 15.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016210; NAD-GDH_euk.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR PIRSF; PIRSF000184; GDH_NAD; 1.
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|PIRNR:PIRNR000184};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184,
KW ECO:0000313|EMBL:CAM66827.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008153}.
FT DOMAIN 633..915
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1020 AA; 115259 MW; 2350976B4F0DF4E2 CRC64;
MMRYTASRAV ARLCGRAFPA SHTVTAMTLL GFAPLATPGR FASSGATSPL VDRDAIIKAV
TTQAVFDKNI VESLANTFVS GLEKSSYPRN FSQAEMIDHV QGLLTAEARF RMGDSFEYVH
ENHRTAFYIC HNEPQKKLRM LRKMARFVSL NQDPHLGSNT HHYISEDRKF AIYNASIEPF
VESGSEEEHV NPKSPALPTQ TAARQLTEEQ KNIIRGLLRR QLSSVFPVFH VEEVEKGHVS
FTMATMVERT NYVASLLSIF QEIEGAEIMM SVSYSFSNGV QVYGFEIRGA TAEQIEERAS
LVGLLPNRPF NAITRLHEAG ALSCEETVFI DAAVIFAMYF TPSPTTDDYR HLKAILAKEP
NGVNRLNNLR SSLTQEVMSE RYTGSVIALY PEFVKLIYED FRLGSTPERR AAIADKITHR
LREDDRPEYD RTLFMSFLKF NEVIIKHNFC KTEKAALAFR LNPVFLKELE FPRVPHGVFL
FAGGQWRGFH IRFTDIARGG VRMIICKERD YRRNKRSVFQ ENYNLAHTQL LKNKDIPEGG
SKGTILVSSR YLNKFDEVRC QHIFLQYVDA LLDVIIPGEK GVVDGLKSEE IIFLGPDENT
AGTFPAAGAL YSKGRGYKSW KSFTTGKDPE LGGIPHDVYG MTTHSVRAYV TSIYEKLGLN
ESEMRKFQTG GPDGDLGSNE LLRSKEKMVG MVDISASLHD PKGIDREELA RLAHHRLPLR
EFNRSKLSPE GFLVLTEDRN VKLPDGSLVE DGSRLRNEFH FLKYSDADVF VPCGGRPRSV
TLENVGRFLK IPNADGESMM EGKYANLSPE QLKFKIIVEG ANLFISQDAR LALEKCGVTL
IKDASANKGG VTSSSLEVFA GLCLSDEEHT KYMSAKSATD APEFYKKYVK EILDRIEENA
KLEFNAIWRE WEKDPQQSKT LIADALSRKN VQIRASMLSS DIFKNRDLVR YVMDQYALKT
LKEVVPVDLM LKRVPENYQH AICAMWLASR YVYQTGVDSN EFDFFRYMTE VYATAAKSAK
//
