ID   K8X6R5_RHOOP            Unreviewed;      1632 AA.
AC   K8X6R5;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=NAD-dependent glutamate dehydrogenase {ECO:0000313|EMBL:EKT77259.1};
GN   ORFNames=WSS_A38366 {ECO:0000313|EMBL:EKT77259.1};
OS   Rhodococcus opacus M213.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1129896 {ECO:0000313|EMBL:EKT77259.1, ECO:0000313|Proteomes:UP000005951};
RN   [1] {ECO:0000313|EMBL:EKT77259.1, ECO:0000313|Proteomes:UP000005951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M213 {ECO:0000313|EMBL:EKT77259.1,
RC   ECO:0000313|Proteomes:UP000005951};
RX   PubMed=23409266;
RA   Pathak A., Green S.J., Ogram A., Chauhan A.;
RT   "Draft Genome Sequence of Rhodococcus opacus Strain M213 Shows a Diverse
RT   Catabolic Potential.";
RL   Genome Announc. 1:E00144-12(2013).
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:EKT77259.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJYC02000160; EKT77259.1; -; Genomic_DNA.
DR   RefSeq; WP_005264315.1; NZ_AJYC02000160.1.
DR   Proteomes; UP000005951; 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;
FT   DOMAIN          29..169
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          398..493
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          546..616
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          737..1239
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1285..1620
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1632 AA;  179152 MW;  6EB7E1E678497F77 CRC64;
     MTESAALKDA EWARDLPEGL RSQVPTLAAV YFRHVDRGDS ESAVNGASGA VLGAHLTLAL
     HRPPERAVTR VYRPGDGREL GASLQIVTDD MPLLVESITA LLNRLGIGIS EFVHPIISVR
     RDPIGALRGI LMGDKAKDAD EDAVSESWIH VQLDPRADAA VLDTLEKEVG TVLADVRQVV
     RDTDIMRKLE RTLADELETS TPCPGVTKDD LEDCADLLRW MSQGNYAALG YRRFELGEPD
     SSGARSLQVV PGSGLGLLRS DTVTEGPLSL PPAAEIPDRP LLVLTQGSFP ATVHRSVYPF
     FVGVSILDEN GNITGEHRFL GVFTVTALHE NVLDIPVIAR RVRKVIDRAG FQLNSYSGQA
     MLEVIQSFPR TELFSSDADT LFDTVTAVHS IGLRRQVRLF VREDFLGRFV SCLIYLPRDR
     YTTRVRLAMQ DILLREFGGG TLEYTARVTE SDLALLHVTI RKSAEQMGSR LDLSDADRER
     VQGMLAEASR SWDDHLGDLL PVTTGVDPVL AQRYAAVLPE GYKEDFDATR ALSDLARLEA
     LEDGSIDLLL YRDPGAEVGH WRFTLYVGGE GISLSQVLPV LQSLGVEVLD ERPYLIPRPD
     GLSCWIYDFG LSVPAELLRS SVEDDLDAEL AAEEASAAPK LQERFTDAFT AVWFGRAEAD
     RFNELILRAG VSWRQAVILR AYAKYLRQAG FPYSQFHIEG VALANPRSAY TLVELFEAMF
     DPETPSPDLV AELDTRLREY IDAVVSLDAD RILRGLFGLI KSTLRTNYFV VGRTGEPPSY
     LSIKLDPTSI QELPKPRPKY EIFVYSPDVE GVHLRFGSVA RGGLRWSDRR EDFRTEILGL
     AKAQAVKNAV IVPVGAKGGF VVKNPPTPSG DAAADRAAAL EAGQDCYRTF ICGLLDLTDN
     VDQASGEIVP PARVVRRDGD DRYLVVAADK GTAKFSDLAN SVAEQYKFWL GDAFASGGSA
     GYDHKGMGIT ARGAWESVKR HFREMGVDTQ TQDFSAVGVG DMSGDVFGNG MLLSRHIRLV
     AAFDHRHIFL DPEPDAARSF AERSRMFALP RSSWADYDTG IISEGGGVWD RTRKSVPISA
     AARTALGLDD AVTELSPPEL VRAILRAPVD LLWNGGIGTY VKASTETNAM VGDKSNDSVR
     VDGNEVRAKV VGEGGNLGVT ALGRIEYSQN GGRINTDAID NSAGVDCSDH EVNIKILLDS
     LVSSGGLPRE ERNPLLASMT DEVAHLVLAN NIAQNNLLGV SRTSAVPMLS VHRRQIEHLA
     SRRGLDRKLE ALPTDEEIAR RRQAGQGLTS PELATLTAHV KLALKDDLLA TDLPDSETFA
     PRLPRYFPTV LRKRFRTAIK AHPLRRQIVA TMLANETIDN GGITFAYRLA DEAGASSTDA
     IRAYAAVTEI FALPELWSRI RSANIAADIE DDLILESGRV LDRASRWFLT NRPQPLAVGA
     EIARYSADFR ALSPRVPQLV RGHQLADVET RARPLVVRGA PEDLAFEVFR LLDKFCLLDI
     SDIADIAERD IDEVAELYYE LDAHLGIDWL LSAVSTLARG DRWHSLARLA LRDDLYSSLR
     QLTMEVLLGG EPHETPQEKI DDWESTNASR LARARSALTE IFESGTLDLA TLSVAARQVR
     SMVRGMGTRS EV
//