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Database: UniProt
Entry: A0A0M8TSU1_9ACTN
LinkDB: A0A0M8TSU1_9ACTN
Original site: A0A0M8TSU1_9ACTN 
ID   A0A0M8TSU1_9ACTN        Unreviewed;      1643 AA.
AC   A0A0M8TSU1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:KOU70764.1};
GN   ORFNames=ADK57_11825 {ECO:0000313|EMBL:KOU70764.1};
OS   Streptomyces sp. MMG1533.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU70764.1, ECO:0000313|Proteomes:UP000037741};
RN   [1] {ECO:0000313|Proteomes:UP000037741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-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:KOU70764.1}.
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DR   EMBL; LGDG01000086; KOU70764.1; -; Genomic_DNA.
DR   RefSeq; WP_053749364.1; NZ_LGDG01000086.1.
DR   STRING; 1415546.ADK57_11825; -.
DR   PATRIC; fig|1415546.3.peg.2580; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000037741; 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:UP000037741}.
FT   DOMAIN          47..193
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          428..520
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          578..647
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          757..1254
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1300..1636
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
FT   REGION          17..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1643 AA;  183371 MW;  4D077C2C7B66C635 CRC64;
     MQTKLDEAKA ELLERAARVA ENSPVGGHLP TGTTDESTPD RDTVLAFLQR YYLHTAPEDL
     ADRDPVDIFG AALSHYRLAE NRPQGTANVR VHTPTVEGNG WTCSHSVVEV VTDDMPFLVD
     SVTNELTRQG RGIHVVIHPQ VIVRRDVTGR LIEVVTAPVA GELPHDAHIE SWIHVEIDRE
     TDRGDLKQIN SDLLRVLSDV REAVEDWEKM RDSALRMADE LPKEPVASDL REQDIEEARE
     LLRWLSADHF TFLGYREYQL REDDSLVAVP GTGLGILRSD PHHAGGDSHP VSPSFERLPA
     DARAKAREHK LLVLTKANSR ATVHRPSYLD YIGVKKFDAD GNVVGERRFL GLFSSAAYTE
     SVRRVPVIRR KVEEVLERAG FSPNSHDGRD LLQILETYPR DELFQTPPDE LQSIVTSVLY
     LQERRRLRLY LRQDEYGRYY SALVYLPRDR YTTGVRLRII DILKEELGGT SVDFTAWNTE
     SILSRLHFVV RVPQGTELPQ LSDADKDRIE ARLVEAARSW ADGFGEALNA EFGEERAAEL
     VRRYGNAIPE GYKADHNPRS AVADLAQLEK LTEEKGFSLS LYEPVGAAPE ERRFKIYRKG
     ESITLSAVLP VLNRLGVEVM DERPYELRCS DRSVAWIYDF GLRMPRPKSG SGDYLGDDGR
     ERFQEAFAAT WTGRAENDGF NALVLSAGLN WRQAMVLRAY AKYLRQAGST FSQDYMEDTL
     RHNVHTTRLL VSLFEARMSP DRQRAGHELV DALLEELDAA LDQVASLDED RILRSFLTVI
     KATLRTNFFQ EAAGGKPHDY VSMKFDPQAI PDLPAPRPAF EIWVYSPQVE GVHLRFGKVA
     RGGLRWSDRK EDFRTEILGL VKAQMVKNTV IVPVGAKGGF VAKQLPDPAV DRDAWLAEGI
     RSYKTFISAL LDITDNMVAG EVVPPADVVR HDGDDTYLVV AADKGTATFS DIANGVAETY
     NFWLGDAFAS GGSAGYDHKG MGITARGAWE SVKRHFRELD VNTQAEDFTV VGIGDMSGDV
     FGNGMLLSEH IRLVAAFDHR HIFIDPKPDA ATSYAERRRV FELPRSSWAD YDTALISTGG
     GVFPRTAKAI PVNAHIREAL GIEDKVSKMT PADLMKAILK APVDLLWNGG IGTYVKASTE
     THADVGDKAN DPIRVDGADL RVRVVGEGGN LGLTQLGRIE FALHGGKINT DAIDNSAGVD
     TSDHEVNIKI LLNGLVADGD MTIKQRNKLL AEMTDEVGSL VLRNNYAQNT AIANALAQSK
     DMLHAQQRYL RHLVREGLLD RALEFLPTDR QIRERLGAAQ GLTGPETAVL LAYTKITVAE
     ELLHTSLPDD PYLRGLLQAY FPSALREKFG ERIDGHPLHR EITTTVLVND TVNTGGTTYL
     HRLREETGAS LEEIVRAQTA ARAIFRSGVV WDAVEALDNK VEAAVQTRIR LHSRRLVERG
     TRWLLNNRPQ PLQLAETVDF FGDRVEQVWV QLPKLLRGAD LEWYQKIYDE LTGAGVPDEV
     ATRVAGFSSA FPTLDIVSVA DRMGRDPMDV AEVYYDLGDR LHITQLMDRI IELPRADRWQ
     SMARASIRED LYAAHAALTA DVLAVGNGTS TPEQRFKAWQ EKNAPILSRA RTTLDEIQGS
     ETFDLANLSV AMRTMRTLLR THS
//
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