ID K4ICR1_PSYTT Unreviewed; 408 AA.
AC K4ICR1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Glutamate dehydrogenase/leucine dehydrogenase {ECO:0000313|EMBL:AFU68199.1};
GN OrderedLocusNames=P700755_001264 {ECO:0000313|EMBL:AFU68199.1};
OS Psychroflexus torquis (strain ATCC 700755 / ACAM 623).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Psychroflexus.
OX NCBI_TaxID=313595 {ECO:0000313|EMBL:AFU68199.1, ECO:0000313|Proteomes:UP000008514};
RN [1] {ECO:0000313|EMBL:AFU68199.1, ECO:0000313|Proteomes:UP000008514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA Bowman J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFU68199.1, ECO:0000313|Proteomes:UP000008514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA Feng S., Powell S.M., Bowman J.P.;
RT "The complete sequence of Psychroflexus torquis an extreme psychrophile
RT from sea-ice that is stimulated by light.";
RL Submitted (SEP-2012) 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}.
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DR EMBL; CP003879; AFU68199.1; -; Genomic_DNA.
DR RefSeq; WP_015023805.1; NC_018721.1.
DR AlphaFoldDB; K4ICR1; -.
DR STRING; 313595.P700755_001264; -.
DR KEGG; ptq:P700755_001264; -.
DR eggNOG; COG0334; Bacteria.
DR HOGENOM; CLU_025763_7_0_10; -.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000008514; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004417}.
FT DOMAIN 181..408
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 408 AA; 45142 MW; 229E4ACD26EA9182 CRC64;
MKELLTKYED KAPEIVFHWR DSETEAEGWT VINSLRGGAA GGGTRMREGL NENEVLSLAK
TMEIKFTVSG PDIGGAKSGI NFDPKDPRKQ GVLERWYKAV SPLLKSYYGT GGDLNVDEIH
EVIPITESCG VWHPQEGVFN GHFHPTEADK INRIGQLRHG VIKVIENTAY SPDVSRKYTI
ADMCTGFGVA ESVKHYYDIY GGDVKGKTAI IQGFGNVGSA AAFYLSKMGA KIIGILDRDG
GLINKDGYSY EEIKELFLAK EGNTLQSKDL IPFEEANKAF WSLGADIFAP CAASRLVQKD
QIDSLVEHGL EVISCGANVP FADKEIFFGP IMEYADQKAS VIPDFIANCG MARVFAYFME
RKVLMTDEAL FDDISITLKN AIQRTFEQSN DKKYISSHAF EIALKQLL
//
