ID C5L543_PERM5 Unreviewed; 1157 AA.
AC C5L543;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=NAD-specific glutamate dehydrogenase, putative {ECO:0000313|EMBL:EER08102.1};
GN ORFNames=Pmar_PMAR014866 {ECO:0000313|EMBL:EER08102.1};
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:EER08102.1, 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; GG679213; EER08102.1; -; Genomic_DNA.
DR RefSeq; XP_002776286.1; XM_002776240.1.
DR AlphaFoldDB; C5L543; -.
DR EnsemblProtists; EER08102; EER08102; Pmar_PMAR014866.
DR GeneID; 9064265; -.
DR InParanoid; C5L543; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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; 2.
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 57..89
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 759..1027
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
SQ SEQUENCE 1157 AA; 129494 MW; 6FEAEDE2CEDCED3C CRC64;
MFEVKLRSES KADDSVYTAN PGAVGYLLAA AHDGDVDEMR RVLAQNSGLT VNSCDYDKRT
PLHLAAAGGH VEAVRFLLEE GAALTPDRMG MLALHDAVMN NNAAEIRSML AEADLKCPGG
ACYLPPEKAQ MLRNADVSEG AGMSITTEEV ETKMTQVFSI ISKEGVFAPA RLWFEIQYYF
TDLGLHPKYF MHCTSAQIAR HIHCLMAAKK VAQSTGSSSI HFEIEDEQSG FFLTSMDDNQ
VTPTERLLAD YLANCGSGES FSVIFIKSEK PPVVDGNAPL GVFMVDKTRF DTHVGVGDVA
EEEDLQLVAS PFFLQRKSLD SQKLYQNLVH EIMKTRNAVV KLIEAPAHMV RQKGSHVLQF
ALYDVERKGK VFFAEFSECL RAHGVVPQRM YIESFANGVV AYHCYLGAEY SPEKLQDLVK
TLRYVSHFKH SPKRSALVWD LVLKKQITPA QAVFFITAVK FVFTFFPKET AEYLTLAEFT
KANAEMKRKL DDLFLQTMSN AITFERIYDT LVSHYELACL MYDDFKKVAK GECEPFYNAA
LADRIDDEVA HRLEAKILKT ALKLTAHLRM TNFFKSGTAA AIAMRFDGSL LEDRPRSLFP
VIPYGIYMVT GRGFYGFHIR FRDIARGGIR MIRSASTQVY STNASSLLEE NYNLAFTQHL
KNKTFPEGGS KGTILLDLGD QNLETNGRDS FNKYIDALLD CMMPQQTGIF SHLPTPEILF
FGPDENTAGF MDMGAYRAKA RGYLYWKALT TGKSTKLGGV PHDRYGMTTN SVHQYVIDLL
QLLGVDETKI TKVQTGGPDG DLGSNEILIA KDKTVAVVDG SGVAYDPNGL NREELVRLAR
LRIPISNFNK DKLTDDKNAF LYNISDKNID LPNGEHFKTG VELRNVFPQL EYCSGDLFVP
CGGRPATVNM GNIHTMFNSQ KEPKFKYIVE GANLFFTEDA RRVLEKAGVH LFKDASTNKG
GVTSSSMEVF AALCMDPKEH DQLLTIPDVT LPPPEFYQQY VNEILAVIKH NASMEFSAIW
KANHETLAAD GNGYVLKIDA TQLLSKKINT LKEYTMKVFS EKNPENEWLV RAVLRRAIPR
LLLVHCGIDK ILERVPEAYI LAVCATWIAN TFVYKYGLEA SEFAFYQFMR NLEEHAQGET
TPTTMELRKS VPSMGLL
//