ID A0A0C1Y254_9ACTN Unreviewed; 1642 AA.
AC A0A0C1Y254;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:KIF74677.1};
GN ORFNames=QR77_13265 {ECO:0000313|EMBL:KIF74677.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF74677.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF74677.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF74677.1,
RC ECO:0000313|Proteomes:UP000031584};
RA Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT 150.";
RL Submitted (NOV-2014) 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:KIF74677.1}.
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DR EMBL; JTHL01000001; KIF74677.1; -; Genomic_DNA.
DR RefSeq; WP_040021882.1; NZ_JTHL01000001.1.
DR STRING; 1576605.QR77_13265; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000031584; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000031584}.
FT DOMAIN 39..185
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 421..513
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 570..641
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 751..1253
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1298..1635
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT REGION 271..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1642 AA; 182162 MW; A178DF7DB3E3F2E1 CRC64;
MQTKLDEAKA ELLARAARVA ETGSESEGRP DKDVLLAYLQ RYYLHTATED LSGRDPVDIF
GPALSHFRLA ANRPQGTANV RVYTPTVEEN GWTCSHSVVE VVTDDMPFLV DSVTNELSRQ
GRGIHAVIHP QIFVRRDITG KLIEVLPDGP GDDADRAHDT LAESWIHVEV DRESDRSDLK
QITLDLLRVL SDVRETVEDW DKMRGSALRI ADELPTEPTA PDLSDEELEE ARELLRWLAG
DHFTFLGYRE YELTDNDSLT AVPGTGLGIL RADPHHSEDE DHPASPSFSR LPADARAKAR
EHKLLVLTKA NSRSTVHRPS YLDYVGVKKF DDKGTVIGER RFLGLFSSAA YTESVRRVPV
VRRKVAEVLE GAGVSPNSHD GRDLMQILET YPRDELFQTP PDQLRTIVTS VLYLQERRRL
RLYLRQDEYG RYYSALVYLP RDRYTTGVRL RLVDILKEEL GGTSVDFTAW NTESVLSRLH
FVVRVPTGTE LTQLTDADTE RIEARLVEAA RSWADGFGEA LNAEFGEERA AELLRRYGNA
FPEGYKADHS ARSAVADLVH LEALDATDKD FALSLYEPVG AGPDERRFKI YRAGEQVSLS
AVLPVLQRLG CEVVDERPYE LRCADRTHAW IYDFGLRMPK GVTGGGGYPA DDARERFQDA
FAAVWTGAAE NDGFNSLVLR AGLSWRQAMV LRAYAKYLRQ SGSTFSQDYM EDTLRTNVHT
ARLLVSLFEA RMSPGRQRAG TELTDGLLEE LDGALDQVAS LDEDRILRSF LTLIKATLRT
NFFQQADSGD QHSYVSMKFD PQAIPDLPAP RPAYEIWVYS PRLEGVHLRF GKVARGGLRW
SDRREDFRTE ILGLVKAQMV KNTVIVPVGA KGGFVAKQLP DPAADRDAWL AEGIASYKIF
ISALLDITDN LVAGEVVPPK DVVRHDEDDT YLVVAADKGT ATFSDIANDV AVAYNFWMGD
AFASGGSAGY DHKGMGITAR GAWESVERHF RELDHDTQTE DFTVVGVGDM SGDVFGNGML
LSEHIRLVAA FDHRHIFIDP EPNAATSYPE RRRLFDLPRS SWADYDKKLL SPGGGIHPRT
AKSIAVNAHV REALGIEPGV SKLTPADLMK AILGAPVDLL WNGGIGTYVK ASTESNADVG
DKANDAIRVN GEDVRAKVVG EGGNLGLTQL GRIEFARRGA GGEGGRINTD AIDNSAGVDT
SDHEVNIKIL LNGLVTSGDM TVKQRNKLLL AMTDEVGTLV LRNNYAQNTA LANAVTQAPS
LLHAHQRYMR RLVRDGHLDR ALEFLPTDRQ VRDLLNSGKG LSQPELAVLL AYTKITVAEE
LIHTDLPDDP YLIKLLHAYF PAPLREKYAE QIDTHALRRE IITTVLVNDT VNAGGSTFLH
RLREETGASI EEIVRAHTAA RGIFGLSECW DAVEALDNKV SAAVQTRIRL HSRRLVERGT
RWLLGNRPQP IEIAGTIKFF AAGVEEVSAQ MPTMLLGAEL AWYQRLVKEL TDAGAPEELA
VRVAGFSSAF STLDIVAIAD RTAQGPLRVA EVYYDLGDRL KISQLMDRIV ELPRADRWQS
MARASIREDL YAAHAALTSD VLAVGDDNST PEERYRAWEQ KNAAILGRSR ATLEEIQSSD
SFDLANLSVA MRTMRTLLRT HS
//
