ID D6Z8R5_SEGRD Unreviewed; 1580 AA.
AC D6Z8R5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:ADG98345.1};
GN OrderedLocusNames=Srot_1885 {ECO:0000313|EMBL:ADG98345.1};
OS Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS 44985 / JCM 13578).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC Segniliparus.
OX NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG98345.1, ECO:0000313|Proteomes:UP000002247};
RN [1] {ECO:0000313|EMBL:ADG98345.1, ECO:0000313|Proteomes:UP000002247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC {ECO:0000313|Proteomes:UP000002247};
RX PubMed=21304703; DOI=10.4056/sigs.791633;
RA Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT 1076).";
RL Stand. Genomic Sci. 2:203-211(2010).
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DR EMBL; CP001958; ADG98345.1; -; Genomic_DNA.
DR RefSeq; WP_013138798.1; NC_014168.1.
DR STRING; 640132.Srot_1885; -.
DR KEGG; srt:Srot_1885; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_11; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000002247; Chromosome.
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:UP000002247}.
FT DOMAIN 70..152
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 369..459
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 517..580
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 689..1191
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1238..1573
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1580 AA; 171695 MW; B5673EA92906437E CRC64;
MATRIELAGM GRALGELSAE QRSRLDGFAR VYADSADPDL HAMLDHISLG AVRRPGADCA
RAARLRGVPT VFVVTDDAPL LVQSVSSLVE SFGARITALE HPVLAVRRDD GGNLLELVLD
ETEPRAAHAE SWIQATLAPD TPDELVAEID AGLVGVLRDV RHAHADHAAV LGRLRQLADD
LPGQGTDVEL ANASRLLRWL ADDHFVFLGY RSFAPDGDGR WRPDEASGLG VLRERAPQLL
PLSAAPVPGE AVLVVAQSPR PSVVGSSRHP YTVMVREIDA QGALRREHRF LGMFPVSAVH
GNVLDVPVVG ERALKVVASC GVRLDSYSGQ QILEVISGLP RPELFCMGLD MLQKIASCAL
DVADRRGLRL FLRQDPLGER VLAWARLPQD RYTTAVRLAM QDVLLREFGA AAIDYSARVT
ESAAWVFFTV RGPFASEPDC ASANEDRIQA LLAAESRTWA DRLVEEAGLT PATAQWYAEA
LPLSYQEAFT PQRAVEDVNI LQGLSRGGVR VRVEDAADTD GADAALVLYV CGEPVTISKV
LPLMTSLGLA VLFERPHGLR RADGEQCWIY QFGVAAEKRS AQERSGPLSE QGTREKLVDA
MEALWNGESE ADQLGVLTLQ AGLSWREVSL LRVYAQYLRQ IDFPYPSSHI SRVLLRYADT
AVLLVRLFRA TFHPQEASNA ARDRILEELR QAVASVISLD EDRVLLAYLD LIEATLRTNF
FRPEGADGSA PTGGGVIALK LAPRKLVLGS LKNLPKPVPE FEVFVSSPRV QGTHLRFGAV
ARGGIRWSDR VSDFRTEILG LAKAQTTKNA VIVPVGAKGG FVVKRPVPPD ASRAEGLACY
KLFIGALLEL TDNIDPQTRA VVGPPDVVRR DNDDPYLVVA ADKGTATFSD TANEIAKSFG
FWLGDAFASG GSVGYDHKAM GITARGAWES VRRHFWELGV DPQTSDFTVV GVGDMSGDVF
GNGMLRSPHI RLLAAFDHRH VFLDPDPDAA RSFAERERLF QLPRSSWADY DASLISAGGG
VWARGVKAVP LSPQVRAALG LPDEVAELSP PELIRAILKA PVDLLWNGGI GTYIKASGQS
DAEVGDKTND ELRVDGSDVR AKVVGEGGNL GATQLGRIEY ARAGGRINTD AIDNSAGVDC
SDHEVNIKIL LSQLEAAGQL PQDRRALLLE SLTDEVAELV LADNIAQNNE LGFARRTAAQ
FVDVHARQIE ELVSAGRLDR EVEFLPEPES LRERGKAGEG LSSPELSVLL AYAKLSLKHD
LLESDVPDSE MYEPKLRAYF PSGLPAEAKA GVGSHALRRQ IVATLLTNEI VDLGGTTFAF
RMSEESGVCV SDVARSFSAA VEIFDLPQTL GPTRPHEMPA AAADRVLAQV RRLLDRSCRW
LVTNRPQPLA MRSEIARYAP KVKELTELLP TWLRGDDVAS FSALRDSMAR LGAPEALAAR
AARLVYEFRL LDIIDVAELV ERPCAPVGEL YFRIGSELGV DRVLNLANLL PVEDQWQVKA
RLALREELHA ALRSLTLDVM ADSDPAESPE EHIADWRARN SARVNRAQDA LAGVFASQVA
DLAAISVATR WVRSMARGSH
//
