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Database: UniProt
Entry: A0A0N7K084_9PSEU
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ID   A0A0N7K084_9PSEU        Unreviewed;      1588 AA.
AC   A0A0N7K084;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:ALL84348.1};
GN   ORFNames=AD017_06180 {ECO:0000313|EMBL:ALL84348.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL84348.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL84348.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL84348.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
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DR   EMBL; CP012184; ALL84348.1; -; Genomic_DNA.
DR   STRING; 1096856.AD017_06180; -.
DR   KEGG; pecq:AD017_06180; -.
DR   PATRIC; fig|1096856.3.peg.1298; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000066228; Chromosome.
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   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; 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; 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:UP000066228}.
FT   DOMAIN          43..141
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          383..473
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          523..590
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          704..1199
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1245..1584
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1588 AA;  172540 MW;  EDD5C2406700442B CRC64;
     MRAGGEPRPG SGAAAELVRL YTRNTPEAES TGGPELAGPA PVVDAHLALA ARREPGRAVV
     DVTAGPGDAT TVDIVTDDMP YLVESVIAGV GRAGGTVRRV VPPILVVHRG PDGSLVRVDT
     DADPSEPGDA RAESWMHLDV VSAGGLDPER LRAELERTLS DVRQVIDDTA AMTLRARALA
     DDLTGAGSAT APHEGDDVHP TEVAELLRWL VDDHFVFVGY RHYSRREGRL QPDTDTGLGV
     LRPDDAGAAV FLPGEGEEGA EEFGGPLLIT RASERSRVLR AVHPYYVGVR ARDDDGTVTG
     EHRFLGMLTV PARHESVLDI PVVARRIRGA IRRAGFPADS YSGQQMLEVF SVLPRAELFA
     SSERRLQETG VGVLEASGRR AVRLFVHPDP YRRFLSCLVY LPRDRYTTDT RLRITEILRT
     RLGGTDVAYT AQVGDAELAM LHLTVATDPS AEPVAYDLPA LQDHVAEATR TWDDLLVAAL
     GDAGPAARPL LDGVPESYKA GVAPHRAVED LRRLLALDED RPFDLRLYRS ADDDIRFALY
     LGDAPATLTA VLPLLQQLDV DVVDERPYEF VRPDGRRCWL YDFGVRAPQP SGAPAVPTVT
     VEDAGTRFED AFAAAWRGDA ESDRFSALVL RAGLHWREAA VLRAYSRYTR QLGGLFTLQY
     TANVLVAHPQ VAEGLITLFR ARFDPAKPDA AEQEAAHQRA LENVTSLIDQ VSGLDADRIL
     RGLLAVIEAT LRTNWFRDRP FFSFKLDPAA VPDMPLPRPR FEIFVYSPRI EGVHLRFGPV
     ARGGLRFSDR QQDYRTEVLG LVKAQAVKNA VIVPVGAKGG FVVRRPAPAP DHVRECYRTF
     VSGLLDVTDN LLTHADGSTE TLPPPGVVRH DGDDSYLVVA ADKGTATFSD LANSVSEEYG
     FWLGDAFASG GSVGYDHKAM GITARGAWES VKHHFRELDL DTQSQEFTVV GVGDMSGDVF
     GNGMLLSEHI RLVAAFDHRH VFVDPTPDAA TSYAERRRLF ELPRSTWESY DASLISAGGG
     VWPRTAKSVP IGPEIRTALG LPADVTRMSP PELIHAILLA PADLLWNGGI GTYVKASVET
     HAEVGDKAND AIRVDGRDLR VRVVGEGGNL GLTQRGRIEF ARSGGRDGEY GRINTDAIDN
     SAGVDCSDHE VNIKILLDRP VADGTLDRPA RNELLASMTD DVADLVLAHN VAQNDVLGVA
     RAHATAMVAV HGRMVSDLVE RAGLDRELEV LPSTAGFDAL AAADLGLTGP ELATLLAHTK
     LDLTHRLLQT DLPDRPAFEP TLPAYFPAPV RERYDHAVRN HPLRREIIGT RLVNEMVDGA
     GISYAFRLGE EIAAGPDDVV RAYAVTTRVF ALPALWEAVR TADVPVAVAD AVVLESRRLL
     DRVSRWFLTN RPQPLAVGAE INRFAAPIAE LRERLPELLQ GRELDAVKER AAELRAAGVP
     EQLVEPAALS LYAYGLLDVV ELVELSDREK EPRPAAEVAQ LYYAVSEHLG VDQALTAVSR
     LDRGDRWHAL ARLALRDDLY GSLRSITLDA LQESAPGTDV DEAIAAWEQS NASKLSRART
     ALEEIGGSAS LDLATLSVIS RQLRGLAR
//
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