ID J1R8J1_9NOCA Unreviewed; 1633 AA.
AC J1R8J1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Bacterial NAD-glutamate dehydrogenase family protein {ECO:0000313|EMBL:EJJ00519.1};
GN ORFNames=JVH1_1914 {ECO:0000313|EMBL:EJJ00519.1};
OS Rhodococcus sp. JVH1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=745408 {ECO:0000313|EMBL:EJJ00519.1, ECO:0000313|Proteomes:UP000009024};
RN [1] {ECO:0000313|EMBL:EJJ00519.1, ECO:0000313|Proteomes:UP000009024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JVH1 {ECO:0000313|EMBL:EJJ00519.1,
RC ECO:0000313|Proteomes:UP000009024};
RX PubMed=22965106; DOI=10.1128/JB.01066-12;
RA Brooks S.L., Van Hamme J.D.;
RT "Whole-Genome Shotgun Sequence of Rhodococcus Species Strain JVH1.";
RL J. Bacteriol. 194:5492-5493(2012).
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:EJJ00519.1}.
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DR EMBL; AKKP01000035; EJJ00519.1; -; Genomic_DNA.
DR RefSeq; WP_009474094.1; NZ_AKKP01000035.1.
DR PATRIC; fig|745408.3.peg.1802; -.
DR Proteomes; UP000009024; 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 738..1240
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1286..1621
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1633 AA; 179375 MW; 05A8487DCF52ACB3 CRC64;
MTESAALKDA EWARNLPEGL RSQVPTLAAV YFRHVDRGDS ESAVNGASEA VLGAHLTLAL
HRPPERAVTR VYRPGDGHEL GASLQIVTDD MPLLVESITA LLNRLGIGIS EFVHPIVSVR
RDPIGALREI LMGDTAKDAD EGSLAESWIH VQLDPRTDSA VLDTLEKEVG TVLADVRQVV
RDTDIMRKLE RTLADELETS APCPGVSKDD 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 RKSTEQMGSR LDLSDADRER
VQAMLAEVSR SWDDHLGDLL PVTTGVDPVL AQRYAAVLPE GYKEDFDATR ALSDLARLEA
LEDGSIDLLL YRDPGAEVGH WRFTLYVGGD GISLSQVLPV LQSLGVEVLD ERPYLIPRPD
GLACWIYDFG LSVPAELLRS SVEDDLDAEL AAEEASAAAP KLQERFTDAF TAVWFGRAEA
DRFNELILRA GVSWRQAVIL RTYAKYLRQA GFPYSQFHIE GVALANPRSA YTLVELFEAM
FDPETPSPDL VSELDTRLRE YIDAVVSLDT DRILRGLFGL IKSTLRTNYF VVGETGEPPT
YLSIKLDPTS IQELPKPRPK YEIFVYSPDV EGVHLRFGSV ARGGLRWSDR REDFRTEILG
LAKAQAVKNA VIVPVGAKGG FVVKNPPTPS GDAAADRAAA LEAGQDCYRT FICGLLDLTD
NVDQVSGEIV PPARVVRRDG DDRYLVVAAD KGTAKFSDLA NSVAEQYKFW LGDAFASGGS
AGYDHKGMGI TARGAWESVK RHFREMGVDT QTQDFSAVGV GDMSGDVFGN GMLLSRHIRL
VAAFDHRHIF LDPDPDAPRS FAERSRMFAL PRSSWADYDT SIISEGGGVW DRTRKSVPIS
AAARAALGLD DAVTELSPPE LVRAILRAPV DLLWNGGIGT YVKASTETNA MVGDKSNDSV
RVDGNEVRAK VVGEGGNLGV TALGRIEYSQ NGGRINTDAI DNSAGVDCSD HEVNIKILLD
SLVSSGGLPR EERNPLLASM TDEVAQLVLA NNIAQNDLLG VSRTSAVPML TVHRRQIEHL
ASRRGLDRKL EALPTDEEIA RRRQAGQGLT SPELATLTAH VKLALKDDLL ATDLPDSETF
APRLPRYFPT VLRTRFRSAI KAHPLRRQIV ATMLANETID NGGITFAYRL ADEAGASSTD
AIRAYAAVTE IFALPELWSR IRSADIAADI EDDLILESGR VLDRASRWFL TNRPQPLAVG
AEIARYSADF RALSPRVPQL VRGHQLADVE TRARPLVVRG APEDLAFEVF RLLDKFCLLD
ISDIADIAER DIDEVAELYY ELDAHLGIDW LLSAVSTLAR GDRWHSLARL ALRDDLYSSL
RQLTMEVLLG GEPHETPQEK IDDWESTNAS RLARARSALT EIFESGTLDL ATLSVAARQV
RSMVRGMGTR SEV
//
