ID   A0A0F4ITH0_9ACTN        Unreviewed;      1654 AA.
AC   A0A0F4ITH0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:KJY24929.1};
GN   ORFNames=VR44_33915 {ECO:0000313|EMBL:KJY24929.1};
OS   Streptomyces katrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY24929.1, ECO:0000313|Proteomes:UP000033551};
RN   [1] {ECO:0000313|EMBL:KJY24929.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY24929.1};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-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:KJY24929.1}.
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DR   EMBL; JZWV01001146; KJY24929.1; -; Genomic_DNA.
DR   RefSeq; WP_045951482.1; NZ_JZWV01001146.1.
DR   STRING; 68223.GCA_002028425_02806; -.
DR   PATRIC; fig|68223.7.peg.3709; -.
DR   eggNOG; COG2902; Bacteria.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000033551; 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   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;
FT   DOMAIN          48..198
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          434..526
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          584..656
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          763..1264
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1310..1647
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1654 AA;  182942 MW;  4D6A29C69104C318 CRC64;
     MQTKLDEAKA ELLARAARVA ENSPAGGLLP TGSEQGEHPG QGATLAYLQR YYLHTAPEDL
     ADRDPVDVFG AALSHYRLAE ARPQGTANVR VHTPTVEENG WTSSHSVVEV VTDDMPFLVD
     SVTNELSRQG RGIHVVIHPT VVVRRDVTGK LIEILGPDCD AHGPKTARPH DSLVESWIHV
     EIDRETDKAD LKQITGDLLR VLSDVRESVE DWEKMRDAAL RIAEELPNEP TAPDLREYEL
     EEARELLRWL ADDHFTFIGF REYNLVDGDA LAAVPGTGLG ILRSDPVHHG QEDAHPVSPS
     FNRLPADARA KAREHELLVL TKANSRATVH RPSYLDYVGV KKFDAEGNVV GERRFLGLFS
     SAAYTESVRR VPVIRRKVAE VLEGAGFSPS SHDGRDLLQI LETYPRDELF QTPVDKLREI
     ATSVLYLQER RRLRLYLRQD EYGRYYSALV YLPRDRFTTG VRLRLMDILK EELGGTSVDF
     TAWNTESVLS RIHFVVRVPQ GTQLPALTDA DVERVEARLV EAARSWADGF GEALTAELGE
     ERAAELLRKY SGSFPEGYKA DHTPRMAVSD LCHLERLSAS DREFALSLYE PVGAGPGERR
     FKIYREGEQV SLSAVLPVLQ RLGVEVTDER PYELRRSDRV SAWIYDFGLR MPAAGNGDAH
     LGDDARERFQ EAFAAVWTGE AENDNFNTLV LGAGLTWRQA VVLRAYAKYM RQAGSTFSQD
     YMEDTLRNNV HTTRLLVSLF EARMSPGRQS AGTELVDAML EELDGALDQV ASLDEDRILR
     AFLTLIKATL RTNFFQLNSA GEQHSYVSMK FDPQAIPDLP APRPAFEIWV YSPRVEGVHL
     RFGKVARGGL RWSDRREDFR TEILGLVKAQ MVKNTVIVPV GAKGGFVAKN LPDPSVDRDA
     WLAEGIASYK IFISALLDIT DNMVAGEVVP PKGVVRHDGD DTYLVVAADK GTATFSDIAN
     GVAESYGFWL GDAFASGGSA GYDHKGMGIT ARGAWESVKR HFRELGHDTQ TEDFTVVGVG
     DMSGDVFGNG MLLSEHIRLV AAFDHRHIFI DPTPDAATSY AERRRLFELP RSSWADYDTA
     LLSAGGGIHP RTAKAIPVNA QMRAALGIEA GVTKMTPADL MQAILKSPVD LLWNGGIGTY
     VKATAETHAD VGDKANDAIR VNGSDVRAKV IGEGGNLGLT QLGRIEFARS GAGGEGGKVN
     TDAIDNSAGV DTSDHEVNIK ILLNGLVAEG DMTVKQRNKL LAEMTDEVGR LVLRNNYAQN
     VALANGSAQA SSLLHAQQRF MRRLGRDGQL DRQLEFLPND RQIRELLNTG RGLTQPELAV
     LFAYTKITVA DELIHTELPD DPYLRRLLHA YFPGALVAKF PEQVDAHALR REIITTLLVN
     DTVNTGGSTF LHRLREETGA SLEEIVRAQL SAREIFGLAQ VWDAVEALDN KVPADVQTRV
     RLHSRRLVER GTRWLLNNRP QPLQITETVE LFGARVAQVW AELPKLVRGA DLEWYQSVMD
     ELTGEGVPSE LAAKVAGFSS AFPTLDIVAT SDRTGVDPLA VAEVYYDLAD RLEITQLMDR
     IIELPRSDRW QSMARASIRE DLFAAHAALT ADVLSVGEAD ATPEERFKAW EEKNAALIGR
     ARTTLDEIRG SDDFDLANLS VAMRTMRSLL RAHG
//