ID   D5V4J4_ARCNC            Unreviewed;      1064 AA.
AC   D5V4J4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:ADG92899.1};
GN   OrderedLocusNames=Arnit_1241 {ECO:0000313|EMBL:ADG92899.1};
OS   Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS   7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Arcobacter.
OX   NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG92899.1, ECO:0000313|Proteomes:UP000000939};
RN   [1] {ECO:0000313|EMBL:ADG92899.1, ECO:0000313|Proteomes:UP000000939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC   {ECO:0000313|Proteomes:UP000000939};
RX   PubMed=21304714; DOI=10.4056/sigs.912121;
RA   Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA   Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL   Stand. Genomic Sci. 2:300-308(2010).
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DR   EMBL; CP001999; ADG92899.1; -; Genomic_DNA.
DR   RefSeq; WP_013135044.1; NC_014166.1.
DR   AlphaFoldDB; D5V4J4; -.
DR   STRING; 572480.Arnit_1241; -.
DR   KEGG; ant:Arnit_1241; -.
DR   eggNOG; COG2902; Bacteria.
DR   HOGENOM; CLU_003404_2_0_7; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000000939; 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; IPR048381; GDH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028971; NAD-GDH_cat.
DR   InterPro; IPR049064; NAD_Glu_DH_ACT3.
DR   InterPro; IPR007780; NAD_Glu_DH_bac.
DR   InterPro; IPR049056; NAD_Glu_DH_HM3.
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; PF21077; GDH_ACT3; 1.
DR   Pfam; PF21074; GDH_C; 1.
DR   Pfam; PF21078; GDH_HM3; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000939}.
FT   DOMAIN          40..100
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          204..690
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          739..1060
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
FT   COILED          191..218
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1064 AA;  121822 MW;  808E4EBBD1B6957F CRC64;
     MATSDMNAVC SQLLRPQDLE ISDELFTQVQ TQNIVTKILE ENNSVNIKIF STYQLYLSLV
     TPILHDIGFL IVDEVTYNIQ NGKDQIFVSR FNLKLENDNA LKEIINAKDN LEKIITKVIS
     DECIQHSKVF SLVYSENLDD RKIKLVRAMI EYIDQAVLTI NSVTILNAYI SHHNITKLFV
     DYFYTKFDPS IKKREVQLKE LKEKIEEEIK QIPQIIDDRI LKLTLSFLDS LIRTSYFLNK
     ETIAFKINAL EFGENLKGLQ PNLENFIYHE SFFGIHLRMS NISRGGLRWS DRHDDYRQEI
     KSLMITQEGK NSIIIPDGAK GGFVINKDTT EVTKEYFKEI YTMFINANLD LVDNMVDGKV
     VKDKNLVCYD GDDAYFVVAA DKGTADMSDV ANEIAISRGF WLGDAFASGG SNGYGHKELG
     ITARGSLKSS ERFFIEEGID IYKDNITVMG IGSMNGDVFG NGLIESDKFI LYGAIGHKEI
     FVDPTPDPIE SFKERKRLFE SKNGSWKNYN KKLISKGGGI FLRSEKEIEL SPEIKKLVGT
     TKKIVSGEEL CIMLLTMPVD LLFNGGVGTY VKASDENSLD IGDKQNEAVR VDGNNLKAKI
     VCEGGNLGFT QKARIEYALG GGRINIDGID NAAGVDTSDH EVNLKILLNM IRIKENICKE
     DSQATLNSMT DQVVKLVLDS NYNQSLAISI DERFSRKYLN DFLKVIEILD NNIPAFNRTA
     FYIPKNENIN EIIDINGSIV RPVLCSLLSY SKIFLKKVLL ESTLVDEQFA LQFLYRYFPK
     SFVGTYEHEI LNHPLKREII ATMMADIIVN SQGCTFVSDY EKLGIERYLL KIKSYLIAKQ
     LFGAKEIREK IYQQDYIMKV DEQYRLINKL EYILYASTRW MVKYLKKNQL DATHILDHKD
     ELFALLKEVH NQKIENLIDK DDEFNLFFSV IDYLRFAVPA IVIKESTNNS FKDVIILFYS
     LIHEFNILDI IISLNKVEIT SKNDVVLRNQ VLQFVEFIVV HYTKKVLNFQ RVNEAPDVAF
     SNFVNNESDS FYKVREHLDL FLTKENKDIK EIAVTVNQMM VSLL
//