ID   A0A0M8WC78_9NOCA        Unreviewed;      1648 AA.
AC   A0A0M8WC78;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:KOV82740.1};
GN   ORFNames=ADL03_23605 {ECO:0000313|EMBL:KOV82740.1};
OS   Nocardia sp. NRRL S-836.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV82740.1, ECO:0000313|Proteomes:UP000037746};
RN   [1] {ECO:0000313|Proteomes:UP000037746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV82740.1}.
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DR   EMBL; LGDY01000104; KOV82740.1; -; Genomic_DNA.
DR   STRING; 1519492.ADL03_23605; -.
DR   PATRIC; fig|1519492.3.peg.5063; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000037746; Unassembled WGS sequence.
DR   GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR048381; GDH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028971; NAD-GDH_cat.
DR   InterPro; IPR049062; NAD_Glu_DH_ACT2.
DR   InterPro; IPR049064; NAD_Glu_DH_ACT3.
DR   InterPro; IPR007780; NAD_Glu_DH_bac.
DR   InterPro; IPR049059; NAD_Glu_DH_HM1.
DR   InterPro; IPR049058; NAD_Glu_DH_HM2.
DR   InterPro; IPR049056; NAD_Glu_DH_HM3.
DR   InterPro; IPR024727; NAD_Glu_DH_N_ACT1.
DR   PANTHER; PTHR43403; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43403:SF1; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR   Pfam; PF05088; Bac_GDH_CD; 1.
DR   Pfam; PF21075; GDH_ACT1; 1.
DR   Pfam; PF21076; GDH_ACT2; 1.
DR   Pfam; PF21077; GDH_ACT3; 1.
DR   Pfam; PF21074; GDH_C; 1.
DR   Pfam; PF21073; GDH_HM1; 1.
DR   Pfam; PF21079; GDH_HM2; 1.
DR   Pfam; PF21078; GDH_HM3; 1.
DR   PIRSF; PIRSF036761; GDH_Mll4104; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000037746}.
FT   DOMAIN          50..196
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          420..509
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          566..642
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          749..1250
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1295..1644
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1648 AA;  181680 MW;  2AB3676BFDB39407 CRC64;
     MTSTGAPTRT DDVSAVSTAD GGSRPASPEQ VRDELIERAA ANAPELADLI RLFYRHVPAE
     EVNDDDPVDL VGAVRSNYQL AESRVPGRAA VRILNPTRSQ DGWQCPVTVV QVVTDDMPYL
     VDSVASELTR GGVQVQRVVH PIVVVRRDPV TGERLEVLPT ADPADPPADA LAESWMNIEV
     DLLTDADRAR ELESRLLSVL TDVREVVEDT DRMASTALQL ADELEKDTSN EACADAAKLL
     RWLADGHFTF MGYRQYELVE EDNDPALRAV LASGLGVLRQ DSLAARRLTE GPDNGAQALS
     PELLVLTQAS AQSSVHRSVY PYYVGVKTFD AAGNVTGEHR FLGIFSTTAL HEDVLDIPVI
     ERRVRDVIHR AGFPLQSYSG QRMLEVIQNY PRTELFSVDE EWLYQTTTGV IALAERRRLR
     LFLRRDPYGR FFSCLVYLPR DRYTTTSRLA MQEVLLAELG GLNLEYSARV GESALARVHF
     MVHRDPQRTL EPDTQAIQLK LAEAVRSWDD RMVEAVGGGH GELGAESATE QGQRFAAVFP
     EAYKEDFPAS TGLEDYRRIE ALVEGDLDMV FYVPDNAEPG ERRFKLFVTG DGITLSDVLP
     MLQRMGVIVV DERPYEIARE DGVRCWIYDF GLRIDKAALA QLSEADLEHV RVRFQDAFAA
     VWRGEAEVDR FNSLVLQGGL TWQQAAMLRA YTKYLRQAGT PYSQDYIEDA VLGHTSVAIA
     LVALFEARFD PRLDEATRTD RTETMVVEIG KLIDDVTSLD ADRILRSLLA LINATLRTNY
     FFRGADGNAR PYLSVKLDPQ AIPDLPAPRP KFEIFVYSPR VEGVHLRFGS VARGGLRWSD
     RREDFRTEIL GLVKAQAVKN AVIVPVGAKG GFVVKKPIAP TGDPGIDREN FMSEGIACYK
     MFISGLLDLT DNLINNEVVP APQVVRYDGD DTYLVVAADK GTATFSDIAN GVSQSYGFWL
     GDAFASGGSI GYDHKAMGIT AKGAWESVKR SFRELGLDTQ TEEFTVVGIG DMSGDVFGNG
     MMLSEHIRLV AAFDHRHIFI DPNPVAATSF AERVRLFSVP RSSWDDYDRS LISEGGGVFP
     LTAKSIPISE QARVALGLPE GVVKLSPPEL KKAVLLAPVD LLWNGGIGTY VKASTESHAD
     VGDKANDAIR VNGADLRVKV VGEGGNLGLT QRGRIEFART GGKVNTDALD NSAGVDCSDH
     EVNIKILLDH LVRDGSVEQQ QRNEVLAEMT DEVGELVLAD NYSQNNVLGV SRAHAVPMLS
     VHARLTADLE ARGALNRELE ALPSAAEFKA LEKRGEGLTS PELATLLAFT KLTLKEELLQ
     SDIPTIDTFA RKLPDYFPSL LRERFGAAIP NHPLARQIIT TVVVNEVVDG GGISFAFRLA
     EEMSASATDA VRAYAVVTQV FDLPSIWREI EALDNVVATE VQDSMVLETR RLLDRASRWL
     LSNRPQPIPV GSTINRFRGV VEELSPFALE LLQGKEYAVV ADKADRYVEQ GVPAELARRV
     AALLYMYGLL DVTEIAELAE REIGPAGGIG PERSHRETAE LYFALSDHLD IDHMLDSVTN
     LERGNRWHAL ARLALRDDFY SSLRAITLDV LRASDLGDTA AEKITKWEQA NASRLGRSRG
     ALEEINRVHQ LDLATLSVAA RQVRSMVR
//