ID I0HH93_ACTM4 Unreviewed; 1645 AA.
AC I0HH93;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:BAL92380.1};
GN OrderedLocusNames=AMIS_71600 {ECO:0000313|EMBL:BAL92380.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL92380.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL92380.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AP012319; BAL92380.1; -; Genomic_DNA.
DR RefSeq; WP_014447265.1; NC_017093.1.
DR STRING; 512565.AMIS_71600; -.
DR KEGG; ams:AMIS_71600; -.
DR PATRIC; fig|512565.3.peg.7167; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_11; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000007882; 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 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000007882}.
FT DOMAIN 68..207
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 436..526
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 582..659
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 767..1255
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1301..1637
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1645 AA; 182576 MW; 380B3A76F347E19D CRC64;
MAVADEAATD SDHTVPDPSV PQPGLALTGR LGASTDSGEL DEPLPNAERL VAQAVQQAGE
DISTASLVDR FWRFAPDEEL VGYTPDEMYA AAVEHRELAR NRLPGEVKLS VTEPSGSQGH
TVVRIVTDDM PFLVDSVMAL LTAHNLQVHL LVHPLIVVRR EPLGALAQVE PEVEPDDAID
GDLVESWIRI EVDPVRRPEA REQLTNEVRR VLTDVRDAVE DWPRMRQRAL MISAELASAT
ESGTMPPVPD KDVTDTIELL EWLAHDHFTF LGYREYHLDE GVLSAVPGTG LGIMRGASKP
RPLATMAPEA YQRVLEKRLL VITKANSRAT VHRSAYLDYI GVKIFDASGT VVGERRFLGL
FSSSAYRTSV RQLPVVKRKV MEVLERSGLS PRGHSGKDLL QILETYPRDE LFQIKTDDLY
EAVIGVLRMA GRRQLRLFLR RDGYGRFISC LIYLPRDRFT TGNRLRMQEI LLRELNGVGV
DYTTRVTERM LARVHFIVRT DPGDPPGHVD PNELAELLAD ATRMWDDDFS LVLERKLGDE
QAKTLFNRYS AAFPESYKNG HTPYEGIQDL AKLELLEEPG QLAMHLFRRR RLGADGVPEP
DERDVRFKVY RYGEPMMLST VLPVLHSLGV RVTDERPYEI RRDDGVIYLY DFGLLPPAGH
RELAEVRPQV ENAFAAAWRG EAEVDGFNEL VLRAGLTWRQ VVVLRAYAKY LRQTGNVFSQ
RYVESTFTAY PEIAGLLVRL FETRFSPALE VGEAERARRA TGLRDRITAL LDQVESLDQD
RILRSYLTLI EATLRTSFFQ RGTEGRPKSY VAFKLDPQAI PDLPQPRPKY EIFVYSPRFE
GVHLRFGAVA RGGLRWSDRR EDFRTEVLGL VKAQMVKNAV IVPVGAKGGF VLKQKPGDRD
EAVECYKGFI TALLDVTDNI LSGKIIPPQD VVRHDGDDPY LVVAADKGTA TFSDIANEIS
VSKDFWLGDA FASGGSAGYD HKKMGITARG AWESVKKHFR DLGIDTQSED FTVVGVGDMS
GDVFGNGMLL SEHIRLVAAF DHRHIFLDPD PDPAISYAER RRLFDLPRSS WADYDRELIS
EGGGVYPRSA KSIPVSPQVR AVLGLGEATS VSPTELMRGI LTAPVDLYFN GGIGTYVKAA
SESHADVGDK GNDAIRINGA DLRVKVVGEG GNLGLTQRGR IEFARSGGRV FTDFIDNSAG
VDCSDHEVNI KILLGGAVTD GEMTLPERDE LLAAMTDEVG ALVLRDNYEQ AMALGNARAQ
AHSLLPVHRR MLKSLEERGE LNRELEALPS DKELAARYET GEGLSAPEFA VLLAYVKISL
EREVLADELV DEGWTADVLT RYFPTPLRDR FAGRMAGHRL RREIISTSLV NEVVNRGGTS
FVYRAMEESG ASAADVIRAY IVVRDVYGLK EIWQAAEGLD NEVPTAAQTA VLLETRRLLD
RAVRWLVSTR RSPIDVAGEI AKLRPGVAEL MPRLPHVIVG AERRNLEQRT AALTGKDVPE
AIAESVSRVF YGFGLLDILE TAASVGRDPH EVASVYFVLS ERFGVDTLLS HISRLPRNDR
WQTLARMALR YDLYAALAAL TAEVLQSTPA EAAPEDRVSE WEQVNAASIA RASNAMGNVE
DSPADLAALS VLLRQIRTLV KTSAA
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