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Database: UniProt
Entry: C5L543_PERM5
LinkDB: C5L543_PERM5
Original site: C5L543_PERM5 
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
//
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