ID A0A010YK74_9ACTN Unreviewed; 339 AA.
AC A0A010YK74;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Glutamate dehydrogenase/leucine dehydrogenase {ECO:0000313|EMBL:EXG80635.1};
GN ORFNames=CryarDRAFT_1719 {ECO:0000313|EMBL:EXG80635.1};
OS Cryptosporangium arvum DSM 44712.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG80635.1, ECO:0000313|Proteomes:UP000021053};
RN [1] {ECO:0000313|EMBL:EXG80635.1, ECO:0000313|Proteomes:UP000021053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG80635.1,
RC ECO:0000313|Proteomes:UP000021053};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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:EXG80635.1}.
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DR EMBL; JFBT01000001; EXG80635.1; -; Genomic_DNA.
DR RefSeq; WP_035849607.1; NZ_KK073874.1.
DR AlphaFoldDB; A0A010YK74; -.
DR PATRIC; fig|927661.3.peg.1690; -.
DR HOGENOM; CLU_025763_0_0_11; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000021053; Unassembled WGS sequence.
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 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:UP000021053}.
FT DOMAIN 137..333
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 80
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-1"
FT BINDING 169..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000188-2"
SQ SEQUENCE 339 AA; 35382 MW; F1BA12DEDC9141EE CRC64;
MSFLRDLRDR DFEQLVVCRD PATGLESVIA IHDTTLGPAL GGVRMRSYAD PEDAVRDAMN
LAQAMTYKSA VAGLELGGGK SVINAPADSP RRDDLLAAHA RFIASLGGRY IPGADMGTGA
ADMDLIARYV PRVSSRRDPS RFTARGVLRA LDAAASWAGV PVRRVAVQGL GKVGSHLVEL
LRARGVDVVV ADVDASRVRG LDAVGVDEIL AADVDVVCPC AAGGVLTEAV IDRLKARVVV
PGANNALAAD ADAAMLAARG IVFVPDFVAN AGGVIACEAE VKGTDDAIEA KIDAIGATTE
SILERASRHG TDPLTEARSL AARRLSTHRP YFPAGDATR
//
