ID C5KN76_PERM5 Unreviewed; 1117 AA.
AC C5KN76;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Glutamate dehydrogenase, putative {ECO:0000313|EMBL:EER14110.1};
GN ORFNames=Pmar_PMAR020892 {ECO:0000313|EMBL:EER14110.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER14110.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
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DR EMBL; GG674563; EER14110.1; -; Genomic_DNA.
DR RefSeq; XP_002782315.1; XM_002782269.1.
DR AlphaFoldDB; C5KN76; -.
DR EnsemblProtists; EER14110; EER14110; Pmar_PMAR020892.
DR GeneID; 9059981; -.
DR InParanoid; C5KN76; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT REPEAT 40..72
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 729..999
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1117 AA; 125214 MW; 56E0B2F64F5AA943 CRC64;
MDSTSIISSF LEAAYEGDLN RMKELMASNS GLSVNVQDYD KRTPLHLAAA GGHMDAVQYL
LGEGAELKTD RFGMLPIHDA VVNHHTDIKE VLGQLDLKCD DAMCYLSPES ENALKEQVKN
TNISLTPEDL EIKMTQVFSI IMKEGVLAAG SLWQEIVYYF TELGLHPSYF KHFTSAEIAR
HIHCLIAAKK VAQATKSDYI HFEIEEADSA FYLTTMEPEK IAITDAKVAE YINTAKDCGY
TITFLKSEKA PMCGGKFPLG IFVVEKQQFE SGVKFEDMME KSDIHLVATS AFLEERSDEV
QKLYQDLIDE TMATRNTVVK VFDAPANLVQ KSGAQVLQFA AFDVDRTGRA YISEINECFR
SHNVEPKRFY VDSFANGIVT YTCFFDPTFQ GEALERLAQT LRYVSHFKHN PRKSGLVWEL
VLNNKITPEH AIFLITAAKF IFSFFPKETE EYLALADYFK SDPSKKSELD TLFRDTMANA
ITYERIYDAL TSNYELTLPM FDDFKKVATG LCKPSYNEEL AAKVDDQVGS RFDAKILKTL
LKLSAHLQMT NFFKAGTASA IAMRFDGEVL ADRPRTLFSR IPYAVYLSSA GASMASTSDS
LRSLVEQTGL QEELRYLLEE NYNLAFTQQL KNKDIPEGGS KGTILMDMDS QNLNTSGRDA
FNSYVDALLD CILAKETGLY SNLSKPEMLF FGPDENTAGF MKLGALRAKA RGYKYWKSLT
TGKSAVLGGI PHDKYAMTTN SIHPYVTELL NKLGVEESKL TKVMSGGPDG DLGSNEILVS
KDKTIAICDG TGVAYDPQGL NREELTRLAH LRVGVANFSR DKLSSDPKAF LVTIDDKDVT
LPNGDHFKSG VEVRNHFPEM EYFSADLFIP CGGRPGTINI GNVDKTMFNP ETKELKFKYV
VEGANLFLTD DARRYLEDAG VQLFKDASTN KGGVTSSSME VFAALCMDTA DHDKFLCSRD
ETSAPPEFYE QYVQEILAAV RHNAKMEFNG IWKTNHEVKY PDGSRYIRKT DATILLSKKI
NDMQSYILGV LEEHDPENDW MVRAVLRRCV PRLLLVHCGL DKIVENTPEA YLNAMVATWI
ADEFVYSNGL QTSEFGFFQF MRSLEEKSEG EVTPSTM
//