ID   A8M2G7_SALAI            Unreviewed;      1685 AA.
AC   A8M2G7;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:ABV99776.1};
GN   OrderedLocusNames=Sare_3986 {ECO:0000313|EMBL:ABV99776.1};
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV99776.1};
RN   [1] {ECO:0000313|EMBL:ABV99776.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205 {ECO:0000313|EMBL:ABV99776.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000850; ABV99776.1; -; Genomic_DNA.
DR   STRING; 391037.Sare_3986; -.
DR   KEGG; saq:Sare_3986; -.
DR   PATRIC; fig|391037.6.peg.4022; -.
DR   eggNOG; COG2902; Bacteria.
DR   HOGENOM; CLU_003404_1_1_11; -.
DR   OrthoDB; 9758052at2; -.
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;
FT   DOMAIN          98..238
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          474..564
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          620..702
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          808..1297
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1341..1676
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1685 AA;  188148 MW;  C54635600A558509 CRC64;
     MDRRPATKPG PDLRQVDTGR DDNFDSATDS DGFGDVETGV TGLTGSSIDS IYDLGLPANA
     LGEDAEDSDL DEPVPNAERL VAQAITLAGD DHDSAALVSR YWRFAPDEEL IGFTAEEMLD
     SVRSHRELAE QRVPGELKLR IHEPDADQHH TVVEIVTDDM PFLVDSVTAL LNSHHLDVHL
     LVHPLLVIRR EPLGRLVEVA AEMEPDDVAA GSLIESWMRI EIDPVRDAED RDNLRRELQR
     VLTDVREAVE DWPKMRQRAL ALADELAAAR NSASRPPVPE KDITDSVELL RWLAHDHFTF
     LGYREYRLVD AAGESGGKAL RAVLGTGLGI LRSDSTESRR LSSMTPEANE RVTEKRLLVI
     TKANSRATVH RSAYLDYIGF KVFDEAGEVV GERRFIGLFA TAAYRTSVRE LPVVRRKVAE
     VVDRSGLSLR SHSGKDLLQI LETYPRDELF QIKTDDLYHA VVGVLRMAGR RQLRVFLRRD
     AYGRFISCLI YLPRDRFTTQ NRLRMQDILL RELNGVGVDY TTRVTESMLA RVHFIVRTDP
     TKPPGDIDAD LLAEELADAT RLWDDDYRLV LERKLGDEQA KHLFARYADA FPEGYKDGHT
     PYEAMKDLAK LELLEESGQL EMHLFRKQLA PRAANRGAGV DEPMDVRFKV YRYGEPMMLS
     AVLPVLHSLG VKAVDEHPYE VERVDGRIWL YDFGLQLPEG HQELTEVRPH VENAFAAAWR
     GEAEVDGFNE LVLRGGLTWR QVVVLRAYAK YLRQAGTIFS QDYMESTFIA YPRIAALLVR
     LFEARFAPGS TSPEQRQQQS RELVAELCAA LDDVASLDQD RILRSYLTLI QATLRTSFYQ
     KRADGRPKSY VALKLDPQAI PDLPAPRPRF EIFVYSPRFE GVHLRFGPVA RGGLRWSDRR
     EDFRTEVLGL VKAQMVKNAV IVPVGAKGGF VLKQKPGDRD EAVVCYKEFI SALLDVTDNI
     VSGEIVPPPD VVRHDGDDPY MVVAADKGTA TFSDIANEIS TAHNFWLGDA FASGGSAGYD
     HKKMGITARG AWESVKRHFR ELGHDTQTQE FTVVGVGDMS GDVFGNGMLL SRHILLVAAF
     DHRHIFLDPN PDAAASWSER KRLFDLSRSS WEDYNAELIS AGGGVFLRTA KSVPISPQVR
     AALGIEEGVS QLSPQELMKA ILTASVDLFW NGGIGTYIKA SSQTNVEVGD KSNDAIRVDG
     KDLRCRVVGE GGNLGCTQLG RIEYAEAGGR VYTDFIDNAA GVDCSDHEVN IKILLNTAVA
     DGELTVGERD ELLAEMTDEV AELVLRDNYD QARAISNAQA QAPSLLPVHR RMIVDLERSG
     ALDRALEALP PDEELAVRME SGMTAPEFAV LLAYVKIVLE KEILAEGLAD EEWTTELLVN
     YFPTPMRERF ADRMSRHRLR RDIVTTMLVN EAINRGGISF VYRVVEETGA TGADVLRAYV
     VVREVFGLRK VWNAVEELDN RVAPELQTGV YLDVRRLLDR AVRWLVTNRR SPIDVPAEIA
     RLRDGVAHLL PGMETLFYGT EREAIAAHIE AMVANGLPRG LAQQAVRLMY SFGLLDVVET
     AASSGRDVSE VASVYFVLSD RFRVDSLLSK ISLLPREDRW QTLARMALRY DLYAALAALT
     TEVLEATPVS LPPVERVQQW EQSNATSIHR AQRAMGEFDE SRADLAALSV LLRQIRTLVR
     TSAAS
//