ID   A0A135LQ34_PENPA        Unreviewed;      1091 AA.
AC   A0A135LQ34;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE            EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN   ORFNames=PGRI_065810 {ECO:0000313|EMBL:KXG51009.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG51009.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG51009.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG51009.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
CC   -!- FUNCTION: NAD(+)-dependent glutamate dehydrogenase which degrades
CC       glutamate to ammonia and alpha-ketoglutarate.
CC       {ECO:0000256|PIRNR:PIRNR000184}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH +
CC         NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.2;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000184};
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|PIRNR:PIRNR000184}.
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:KXG51009.1}.
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DR   EMBL; LHQR01000044; KXG51009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LQ34; -.
DR   STRING; 5078.A0A135LQ34; -.
DR   OMA; LYCLPQN; -.
DR   OrthoDB; 89313at2759; -.
DR   Proteomes; UP000070168; Unassembled WGS sequence.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:UniProtKB-UniRule.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016210; NAD-GDH_euk.
DR   PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11606:SF42; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   PIRSF; PIRSF000184; GDH_NAD; 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   NAD {ECO:0000256|PIRNR:PIRNR000184};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000184};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070168}.
FT   DOMAIN          726..990
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1091 AA;  123108 MW;  BC8CB4C414DA76A6 CRC64;
     MSSPITTPQS ETPNGNGVSL PNRPLPKPYA SQDGSSGSGT PIGFQRYPPH NKHLDHVVGA
     ASRQPSPQPT HLGIPGTPHR VLSEEDPGYI AATFEGKQKQ MEQVMDILEE KGFFPSDFVI
     SETTWFYNKL GIDDTYFQTE TVDAIVTQIL SLYAAKVAAY ARDDKQLEIR LDKEAEDHAV
     YIDTSRPGMA SIDGPRYEQR IDEKYINHSK GANSYRVETF RSPSPLPGDN GQQLRCYFVY
     KCQFANPTPS PNETNIDIIG EKRFLQKATP NTKAIYQEII STAVGRSGPV IEMFEIEGSR
     EKRLVIAYRQ GSAMGLFSAL SDLYHYYRLT SSRKYLENFS NGITVISLYL RPSDNSEISA
     KFPPIEAAIH QIMKEVSLLY CIPQNRFQGH FATGRLSLQE TIYAHCAWVF VQQFLNRLGS
     EYTSLSALLD SNNSVHAELL SKIKKRLRTE TFTADYIFEI INKYPELIHK LYLDFANTHY
     VQTQESGDDF LPTLSYLRLQ VDEVLDGAKL KQLIRGTAMN EHDEMVMTSF RVFNSSILKT
     NFFTPTKVAL SFRLKPDFLP EHEYPQPLYG MFLIISSEFR GFHLRFRDIA RGGIRIVKSR
     NGEAYNINAR SLFDENYNLA NTQQRKNKDI PEGGAKGVIL LDADHQDKAR VAFEKYIDSI
     LDLLLPPVSP GIKDPIVDLH GKDEILFMGP DENTAELVNW ATEHARGRGA PWWKSFFTGK
     SPKLGGIPHD AYGMTTLSVR QYVLGIQRKL NLEPSTLLKL QTGGPDGDLG SNEILLSNEK
     YGAIVDGAGV IYDPNGLNHE ELLRLAKKRA MISEFDMTKL SPEGYRVLVD EKNVKLPSGE
     VVHNGMLFRN TYHLRAQEKF DEFVPCGGRP ESIDLSSVGK LIKDNKCIIP FIVEGANLFI
     TQDAKLRLEK AGCILYKDAS ANKGGVTSSS LEVLASLSFN DEEFVENMCV REDGTVPEFY
     QSYVREVQEV IQSNAALEFE AIWREHQQTG VLRSVLSDRL SLAITKLDEE LQMTELWDNV
     ALRRSVLGDA LPRRLLDKIG LETILERVPE NYLRAIFGSH LASRFVYEYG NQPSQFSFFD
     FMTKRLAKLQ S
//