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
//