ID S7V741_9BACT Unreviewed; 409 AA.
AC S7V741;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glu/Leu/Phe/Val dehydrogenase family protein {ECO:0000313|EMBL:EPR66050.1};
GN ORFNames=ADICYQ_4936 {ECO:0000313|EMBL:EPR66050.1};
OS Cyclobacterium qasimii M12-11B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR66050.1, ECO:0000313|Proteomes:UP000014974};
RN [1] {ECO:0000313|EMBL:EPR66050.1, ECO:0000313|Proteomes:UP000014974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12-11B {ECO:0000313|EMBL:EPR66050.1,
RC ECO:0000313|Proteomes:UP000014974};
RX PubMed=23950138;
RA Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT from Arctic Marine Sediment.";
RL Genome Announc. 1:e00642-13(2013).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
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:EPR66050.1}.
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DR EMBL; ATNM01000159; EPR66050.1; -; Genomic_DNA.
DR RefSeq; WP_020894032.1; NZ_ATNM01000159.1.
DR AlphaFoldDB; S7V741; -.
DR STRING; 641524.ADICYQ_4936; -.
DR PATRIC; fig|641524.5.peg.4891; -.
DR eggNOG; COG0334; Bacteria.
DR OrthoDB; 9803297at2; -.
DR Proteomes; UP000014974; Unassembled WGS sequence.
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; 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 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}.
FT DOMAIN 182..409
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 409 AA; 45000 MW; EF4C420C24AE0EEE CRC64;
MRELLKKFEN MQPEIVFEWS DSETEAEGWL VINSLRGGAA GGDTRMKPGL DKNEVIQLAK
NTAIKNTVSG PAIGGAKSGI NFNPSDPRKA GVLERWFKVV SPILKSYYGT SAGINIDETT
ELIPITEEYG LWHPQEGIVN ALYNKGGEPK KIRKIGQLRQ GLSKIVENPK YLPASQIKFQ
ISDVITGYGL SEAVQHYYKL WGGTASGKKA IIQGWGNVGA AAAYFLAKEG VQIIGIMSLE
GAIIDKNGLS PEEITSLFLN KEDNKLRSEK LISFESAKDK IWDLPTDIFI PAAKSRLIQK
DHLNKLIKGG LELIVCGANF PFVENDIFLG PVTKMADDRV SLIPDFISNA GLARIAAYLM
SDKAQITDEA MFQDVSKTVF RALKKCHTFN PQKTKIAQTA LEIALQKLQ
//
