ID   V6JT29_9ACTN            Unreviewed;      1666 AA.
AC   V6JT29;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:EST22266.1};
GN   ORFNames=N566_26735 {ECO:0000313|EMBL:EST22266.1};
OS   Streptomycetaceae bacterium MP113-05.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae.
OX   NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST22266.1, ECO:0000313|Proteomes:UP000017915};
RN   [1] {ECO:0000313|EMBL:EST22266.1, ECO:0000313|Proteomes:UP000017915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP113-05 {ECO:0000313|EMBL:EST22266.1,
RC   ECO:0000313|Proteomes:UP000017915};
RA   Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces bacterium from a marine sponge: physiological
RT   characterization and genome-based analysis of secondary metabolite
RT   biosynthesis potential.";
RL   Submitted (SEP-2013) 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:EST22266.1}.
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DR   EMBL; AWQV01000865; EST22266.1; -; Genomic_DNA.
DR   STRING; 1380770.N566_26735; -.
DR   PATRIC; fig|1380770.3.peg.4666; -.
DR   HOGENOM; CLU_003404_1_1_11; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000017915; 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:UP000017915}.
FT   DOMAIN          42..197
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          439..531
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          603..674
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          780..1277
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1323..1659
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1666 AA;  185656 MW;  373C88CF6A567D96 CRC64;
     MQTKLDEAKA ERLAEAVRVA EQSSLGGQKT KGLRPDSVGA YLQRYYLHTA PEDLTDRDPV
     DILGAALAHH SLAQDRPQGT ADVRVYTPSV DENGWACTHT VVEVVTDDMP FLVDSVTNEL
     SREGRGIHVV VHPQMVVRRD VAGTLLEVLD AGRDPYSPAA STHRPEELPD DAVSESWIHV
     EIDRETDRED LHAIRESMLS VLSDVREAVE DWTKMREAAL RIADGLPDEN TPGDLHEGEL
     EEARELLRWL ADDHFTFLGY REYELEVEGE GDGELLLAAK PGTGLGVLRS DPRHVDDEGH
     PVSPSFNRLP ADARAKAREH NLLILTKANS RATVHRRSYL DYVGVKKFDA AGNVVGERRF
     LGLFSSAAYT ESVRRVPVIR RKVAEVLSSA GFTPDSHDGR DLMQILETYP RDELFQTPVD
     ELRNIVTSVL YLQERRRLRL YLRQDEYGRY YSALVYLPRD RYTTAVRLRL IDILTEELGG
     TSVDFTAWNT ESILSRLHFV IRVKPGSALS ELTDEETDRI EVRLAEAARS WADGFTEALV
     AECGEEHAAE LGHRYANAFP EGYKADFPPR AAVADLQHIQ KLRGAGRATG GEEQGSEEHL
     PDFSLSLYEP VGAAQGERRF KIYRTGEPVS LSAVLPVLQA LGVEVVDERP YELRAVDRSR
     AWIYDFGLRM PASQMKSFGD DARERFQDAF SAVWTGRAEN DGFNTLVFTA GLTWRQAMVL
     RAYAKYLRQA GATFSQDYME DTLRHNVHTT RLLVNLFEAR MSPERARAGH ELIDAMLEEL
     DAALDEVASL DEDRILRSFL TVIKATLRTN YFQRDTFGEP HAYVSMKLDP QQIPDLPAPR
     PAYEIWVYSP RVEGVHLRFG KVARGGLRWS DRREDFRTEI LGLVKAQEVK NTVIVPVGAK
     GGFVGKQLPD PAEDRDAWQA EGIACYRTFI SGLLDITDNL VAGEVEPPRD VVRHDEDDTY
     LVVAADKGTA KFSDIANEVA TAYGFWLGDA FASGGSAGYD HKGMGITAKG AWVSVERHFR
     ELGHDTRTQE FTVVGIGDMS GDVFGNGMLL SEHIQLVAAF DHRHIFLDPD PDAATSYAER
     RRVFDLPRSS WEDYDTSLIS AGGGVHSRRA KSVPVTPQVR KALGIESGVS KMTPADLMRA
     ILSAPVDLLW NGGIGTYVKA STETDADVGD KANDAIRVDG QDLRVRVVGE GGNLGLTQLG
     RIEYAHQGGR INTDAIDNSA GVDTSDHEVN IKILLNAVVA AGDMTVKQRN ALLAEMEEEV
     GELVLRNNYA QNAALANSLE QASSLLHAHQ RHMKRLVKEG KLDRQLEFLP SEKQIRERLS
     GDLGLTQPEL AVMLAYTKIV ITEDLLSSDL PDDPYLQQLA LAYFPQALCE RFEQEIHEHA
     LRRQIISTLL VNDTINTGGS SFVHRMKEES GASAEEIVRA HTAARAIFGL ADIWDEVESL
     DNKVSADVQT RIRLHSRRLV ERAARWLLNN RPQPLQLTET IELFGERVAT VWAELPKLLQ
     GDDLEWHRKV HDELAGAGVP EDLARKVAGF SAAFPALDVV AVAERTGDGL LDVAEVYYDL
     ADRLGITELQ ERVGELPRSD RWQSMARAAI REDLYAAHQL LTADVLASTD DRTSAGQRFE
     AWEEKNSAIL HRARATLEEI HASESFDLAN LSVAMRTMRT LLRSNR
//