ID A0A177DJR7_ALTAL Unreviewed; 1065 AA.
AC A0A177DJR7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=NAD-specific glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000184};
DE EC=1.4.1.2 {ECO:0000256|PIRNR:PIRNR000184};
GN ORFNames=AA0117_g5163 {ECO:0000313|EMBL:RYN77058.1}, CC77DRAFT_938842
GN {ECO:0000313|EMBL:OAG19099.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG19099.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG19099.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG19099.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN77058.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN77058.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
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}.
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DR EMBL; KV441482; OAG19099.1; -; Genomic_DNA.
DR EMBL; PDXD01000010; RYN77058.1; -; Genomic_DNA.
DR RefSeq; XP_018384520.1; XM_018534643.1.
DR STRING; 5599.A0A177DJR7; -.
DR GeneID; 29120237; -.
DR KEGG; aalt:CC77DRAFT_938842; -.
DR VEuPathDB; FungiDB:CC77DRAFT_938842; -.
DR OMA; LYCLPQN; -.
DR OrthoDB; 89313at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; 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:UP000077248}.
FT DOMAIN 696..960
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 25..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 120033 MW; 502DB8ACE022DFB3 CRC64;
MASTPVDAAN GHPAQHKQLE QLLHTPDRRP SPLPTHLSAP GSGSSTPRMI PQEGSGGSGY
VAPVFEGKAQ QMEAVMDGVE EKGFMPPELV ESETKWFYNE LGIDDMYFAT ETVDAIISHI
HSLYAAKVAA YARDDKRLEI RLDKEAADHA VYIDTSRPGV SVIDGPQYEQ RLGKKYLAVS
KPGLAYRVES FRSESPLPGS EDQQLRCYFV YQCDFVDPNP SETETDIEKI GDKRFLQKAT
KNTKEVYQQI LQVAVERTGP VIDHFDIEGS RDKRLVVGFK RGSALGLFSA LSDLYHYYGL
TTSRKYVEQF SNGYTVMSLY LRPLPGAAGA KHPPIEASIH QITKEVSLLY CLPQNKFQTL
FATSRLSLQE TIYAHCVWVF ITHFLNRLGS EYTALSAILD PENSVHAELL SKLKRRLRAE
TFTADYIYEI IMTYPELVHT LYLPFAKTHY VQTRGQEDDF LPTLSYLRLQ VDKVQTDAEL
TDTINKAVAN DHHEMVMTAF RVFNQSVLKT NFYTPTKVAI SFRLNPTFLP STEYPQPLYG
MFLVIGSEFR GFHLRFRDIA RGGIRIVKSR SQEAYSINAR SMFDENYNLA NTQQRKNKDI
PEGGSKGVVL LDFKHQDKAR GAFEKYIDSI LDLLLPPTSP GIKDPIVDLH GKEEILFMGP
DENTADLVDW ATEHARTRGA PWWKSFFTGK SPKLGGIPHD RYGMTTLSVR EYVLGIYRKL
NLDPSKVRKL QTGGPDGDLG SNEILLSNEK YVAIVDGSGV LVDNNGINHE ELVRLAKERK
MINHFDASKL SPEGYRILVD DTNKRLPNGD LVYNGTTFRN TFHLRSDMHY DSFVPCGGRP
ESIDLSTANK LIVDGKSVIP YIVEGANLFI TQDAKLRLEK AGCILYKDAS ANKGGVTSSS
LEVLASLAFD DESFLKHMCV GEDGQAPEFY NNYVRQVQKT IQNNARLEFE AIWREHQNTG
QPRSVLSDTL SNAITKLDEE LQNTELWHNV EFRESILKEA LPNILLEKIG LDKIIKRVPD
NYLRAIFGSY LASRFVYEYG VSASQFAFFD FMNKRMAKGS KSAAH
//
