ID   W5TP53_9NOCA            Unreviewed;      1633 AA.
AC   W5TP53;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:AHH20904.1};
GN   ORFNames=NONO_c61290 {ECO:0000313|EMBL:AHH20904.1};
OS   Nocardia nova SH22a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH20904.1, ECO:0000313|Proteomes:UP000019150};
RN   [1] {ECO:0000313|EMBL:AHH20904.1, ECO:0000313|Proteomes:UP000019150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH22a {ECO:0000313|EMBL:AHH20904.1};
RX   PubMed=24747905;
RA   Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT   "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT   Analysis of the Complete Genome of Nocardia nova SH22a.";
RL   Appl. Environ. Microbiol. 80:3895-3907(2014).
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DR   EMBL; CP006850; AHH20904.1; -; Genomic_DNA.
DR   RefSeq; WP_025352242.1; NZ_CP006850.1.
DR   STRING; 1415166.NONO_c61290; -.
DR   KEGG; nno:NONO_c61290; -.
DR   PATRIC; fig|1415166.3.peg.6304; -.
DR   eggNOG; COG2902; Bacteria.
DR   HOGENOM; CLU_003404_1_1_11; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000019150; 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:UP000019150}.
FT   DOMAIN          30..168
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          394..487
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          542..609
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          736..1237
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1284..1619
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1633 AA;  179221 MW;  B3F199C6C0ECA008 CRC64;
     MTVSSELSSA AWAESLPEPL RGELATLESA YFRHVDAGDV DCAITGTSAM VFRRHLELGM
     QRPPGAARVR VYHPDDGSGL GAAVQLITDD MRLLVESVAS ALTRIGVTVS EVIHPIFEVL
     RDDQGRLHSA SPHEVDSNGV HGVRESWIHV QLHPSTGRDM LDRIETEIPD VLADVRQVIS
     DTEAMRGVQD RLARELTRTA DAGTAPYSAT DLVDCANLLR WMADGHFTVL GYARFQRDPS
     ASAESKSVVV PDSCLGVLRP DVGTDFRVPV DGGNRPLLML TQGLVPATVH RSVYPYFVGV
     AEADASGAVV GEHLFIGVFT VAALHENVLD IPVIARRVRS VIEECGFDLD SFSGQAMLEV
     IQSFPRTELF SSDIETMRRT ASAVLNVGMR RQVRLFMRRD SYGRFVAAMV YLPRDRYTTR
     VRLEIQDILV RELGGVSIDY SARVSENELA SVYFTVHLPE PGTRVDTSEA NRLRIQNLLA
     EATRTWDDHL RDEVARSSVL DPAVVQRYSA ALPDGYKEDF GPARALADIV RLERLDASAI
     DQHLYRRENA EPGSWRFTLY VGGGISLSQV LPLLQSLGVE VVDERPYEVD FDDGRVVWIY
     DFGLQARPDL LRTALDRDMD AELVETADRL DVLGAQERGL RDRFTDAFDA LWHGRAEADA
     LNELVLRAGL HWRSVSVLRA YSKYLQQADF PYSQAIIARV LLASPQVARL FVELFEAMFD
     PDAASAEQAD QLRAAVRECV NEVVSLDADR ILRAILGVVT ATLRTNYYVV DAEGAAREYL
     SVKVEPHAIA ELPKPRPQFE IFVYSPRVEG VHLRFGAVAR GGLRWSDRLE DFRTEILGLV
     KAQAVKNAVI VPVGAKGGFV VKHPPVPTGD PVADRQALQA EGIACYRTFI SGLLDLTDNV
     DRATGAVLPP ARVVRRDADD TYLVVAADKG TATFSDIANG VAMDYGFWLG DAFASGGSAG
     YDHKAMGITA KGAWESVKRH FAEMDIDTQA EEFTVVGVGD MSGDVFGNGM LLSEHIRLVA
     AFDHRHIFID PDPVAGSSFA ERRRLFGLVR SSWADYDTSL ISTGGGVWDR TVKAIPVSPE
     IRRALGLDDE VVSLSPPEMI RAILCAPVQL LWNGGIGTYI KAGTESNGDV GDKSNDAVRV
     NAGDLRVRVI GEGGNLGVTA LGRIEFCKLG GKCNTDALDN SAGVDCSDHE VNIKVLLDGV
     VETGELPVED RNPLLASMTD DVSEMVLRDN VSQNFLMGMS RTESPRMLNV HTRVIDDLEH
     RRGLDRELEA LPSGKELARR GEAGAGLTSP ELANLLAHVK LSLKADLLDS DLPDSAYFAT
     RLPDYFPEAL RTRFGGAIKR HRLRREIVTT MVINEMVDLG GITYAHRLNE EIGASTTDVV
     RAFAATSQIF DLPALWQRIR AADVQTAVKD ELELETKRTL DRASRWLLSN RPQPVAVGAE
     IHRYSGPVRE LAPKVPGWLR GHHLDTLSES SAAIVSRGVP EDLATEVFGL LNLFPLLDVV
     DIADITDRSG EEVGALYYAL NEHLKIDWLL QAVSHLERGD RWHALARLAL RDDMYGSLRS
     LTLDVLSAGD PEETAEEKIA YWESKNQSRL GRARAALSEL FASGAHDLAT LSVAARQVRS
     MVSGVGAQSE VPR
//