ID E8RNU7_ASTEC Unreviewed; 1596 AA.
AC E8RNU7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:ADU11860.1};
GN OrderedLocusNames=Astex_0159 {ECO:0000313|EMBL:ADU11860.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU11860.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002395; ADU11860.1; -; Genomic_DNA.
DR RefSeq; WP_013477694.1; NC_014816.1.
DR STRING; 573065.Astex_0159; -.
DR KEGG; aex:Astex_0159; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_5; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000001492; Chromosome 1.
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; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001492}.
FT DOMAIN 40..162
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 409..497
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 551..623
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 728..1216
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1263..1590
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1596 AA; 175150 MW; 671C35946677C5BC CRC64;
MDDLSLSTEL DALVADARAG IEAAFTAALT GPADDAARSF LAQCLEDYDP EEMPELSLEE
VGRLFAQSWG RAAVRDGAGA LKTITPVNSA LDVVEIVQPD APFIVESVMG ELIDQGLIIR
SMFHPVVTVN RDDKGQRGSG KAVTESLMLV FVGRQPAEKH AAILSGVERT LNDLRAAVHD
FPRMQALLAE EMTALEALSL HPVVQIDPAV LQEELAFLRW VSENHFVLLG ARTYVYPRSP
DGNYVAEEPL NLLQEEYGVL RDKRAILRRG SEPAILSREL LSHLASSEPV TVAKGNLKSR
VHRRVYMDYI SIKHYGADGK PSGETRFVGL FTSDAYDRPA FEVPLIRKKC DHVLNESRRL
GFNNGGYAEK RLKNILETYP RDELFQIQES DLLRITRGVL HISDRPRVRL FARRDPFDRF
ISVLLYLPRD TYSVSVQERA GQLLAEGFGG RVSALYPFVT GGALSSIHYI IGVTPGGHPD
PNLADIEDRV TDLTLDWAQR VEDAALEAGQ TQTDYVKWAR AIPVAYQERY GIAEAVTDIA
ILAGLDEAHP LTVRAWQPQG ASDRFSLKLY DRAETAIPLS DILPVLERMG LKTLEEFGHR
IESTDVPRHF IHEFIVQLPA AHPTAFADFR EDFEGALMAL WRGETEIDGF NALTLLGLSW
REAALLRALC KYRGQSGLDP SAIVQQQALR AYPDVAAALV YLFDLKFAVN DTPIDTRKVE
VEAALNRINT LLQGVTSLEH DRVLRRLAAL IGAIQRTNYY QNRGYISFKI ASRELADLPD
PKPYREIFVW SPVVEGVHLR FGPVARGGLR WSDRKEDFRT EVLGLVKAQQ VKNAVIVPVG
SKGGFYPKQL PAGGAPDAIR AEAVRAYKMY LSGLLDITDN LDAQGGIIAP KNVVCWDAPD
PYLVVAADKG TATFSDIANG VARDYGFWLD DAFASGGSVG YDHKVMGITA RGAWEAVKRH
FRERGKDIQS ETFTTVGVGD MSGDVFGNGM LLSKQTKLIA AFDHRDIFID PNPDPAVSFA
ERERLFALPR SSWQDYDKAK ISAGGGVFSR GLKSIELTPE IRAALDIQAT SLTPFELMQA
ILRAPAELLY FGGIGTYIKA ASQSHLEVGD KANDAIRVDA GDIRAAVIGE GANLGITQAG
RIALAAQGVK LNTDAIDNSA GVDCSDHEVN IKILLGRLVQ SGRMTLEARD VLLAEMTDEV
GHLVLKDNYA QTLALTLLES TALSDNASMQ AFMTALEKRG KLDRKVEGLP TNAQLEARKA
QNAGLYRPEL AVVLAYGKIV LFDDLIETTA IDDPVFEEAL IDYFPKPLHG FIDDIRAHRL
HREIVATVLC NEMINILGPS FPLRLQKAAA VDAGALALSF EGARRLFETD ALWAEVSALD
AQIPAAAQTA LYNAIATFLR RQVYFIARRF AGRPETLTEV INAYQTGIAT LMSAQGVLSP
NEAARVEARA QKLISAGAPE DLSRRVSALL SWTSAIDMVD LADGGDVVDA ARLYLATGER
FGFDRLRAGA GELYSADPWD RMAIRRLIED IYAEQKSVVA AVRRDAQGLK AWAEAQAAQV
APLQSLLSEI ESTGAGWSFA KLSIVNAALR QWVQKL
//
