ID   F5Z7U9_ALTNA            Unreviewed;      1612 AA.
AC   F5Z7U9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:AEF03142.1};
GN   OrderedLocusNames=ambt_08070 {ECO:0000313|EMBL:AEF03142.1};
OS   Alteromonas naphthalenivorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF03142.1, ECO:0000313|Proteomes:UP000000683};
RN   [1] {ECO:0000313|EMBL:AEF03142.1, ECO:0000313|Proteomes:UP000000683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC   {ECO:0000313|Proteomes:UP000000683};
RX   PubMed=21705606; DOI=10.1128/JB.05252-11;
RA   Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA   Oh T.K., Kim J.F.;
RT   "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT   bacterium Alteromonas sp. strain SN2.";
RL   J. Bacteriol. 193:4292-4293(2011).
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DR   EMBL; CP002339; AEF03142.1; -; Genomic_DNA.
DR   RefSeq; WP_013784080.1; NC_015554.1.
DR   KEGG; alt:ambt_08070; -.
DR   eggNOG; COG2902; Bacteria.
DR   HOGENOM; CLU_003404_1_1_6; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000000683; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          34..177
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          406..494
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          551..630
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          728..1222
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1268..1604
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1612 AA;  183510 MW;  A1DD1559DA8F533D CRC64;
     MTVTSQRHSV LLDNVFALIE KKVDAQQKSL VQQFGRLLYK NISSDDLEDR NDSDLYGATL
     SLWNGLAKFD NSAPYIRVFN PEIEKHGWHS SHTIVEIIVR DMPFLVDSVR MSLNRLNITA
     HWFLHSPIRI KRNDKNQVVE FAEPGKAVEN TRKETVIFIE VDHQSAKKDI DELTKELHSV
     VDEVSLAVKD WQEMTTKLKT VVKDSTKLNW PGSADEKKQT KAYLQWLSDH NFTMMGYRYY
     EVKAIEGDHR WIPSNDTSLG LLKNSINDRE RLLSKLPASA RAEALSQSPL ILTKTNSRAR
     VHRPAYMDYV GVKAFNKDGQ VVGEHRFLGL YSASFYNQSV TQLPMLSEKI QRICDLSGYE
     PGTHAFKAFV NIVETYPRDE LLQTPAEELA QIVMGIFQMQ ERGISRLFIR KDVFGRFFSC
     MVFVPRERYN TQLRVDTQAL LKASLGAKEE VEFTTFFSES VYARTHYIAR VNDNNAEFDV
     KEIERNIIEL TKTWSDRLAS SISAAHGEAQ GKALERKYGN AFSRSYMEQN LPGDALVDIG
     KIEQLDDDHT LDMLFYRPQE EQSDSQIVKL KLFHRAEPIH LSDVLPMLEN FGLRVIDESP
     YKITCPDGLR NWVMDFTMLH KSGQHFDMER AQTLFQDAFA KVWNNDLEDD AFNRLILGAN
     LTGRKVTILR AYAKYMRQTG SSFSRDYIAN TLANYPDIAR LLVEFFDQRI NPKKKRSAKK
     EEALLDNIKT QLDSVSNLDD DRIIRRYLDM MSATLRTNFY QPDEAGNEKS YVSFKMLPEM
     IPDMPLPLPK FEIFVYSPRL EGVHLRGGKV ARGGLRWSDR QEDFRTEILG LVKAQQVKNT
     VIVPVGAKGG FVCKKLPVGE GREAIQAEGQ ACYRTFITSL LDITDNIVNG EIVPPKDVVR
     LDEDDPYLVV AADKGTATFS DIANGIAYEF GFWLGDAFAS GGSVGYDHKK MGITARGGWE
     SVKRHFREIG IDCQTTDFTA VGVGDMAGDV FGNGMLLSKH TKLISAFNHL HIFFDPDPDA
     AASYKERTRL FENPRLSWED YDSALISKGG GIFSRSAKSI KLTPEMKKWL GTRQMSMTPN
     ELIHNILKMP VDLLWNGGIG TYVKSSKESH AEVGDRANDD LRLNGKDVQA KIVGEGGNLG
     LTQLGRIEYA ASGGRVNTDF IDNVGGVDCS DNEVNIKILL NSVVNDGELT VKQRNNLLHD
     MTDDVSRIVI KDCYRQTQSI SITEMSGVSL LKEQLRFIHG LEREGQLNRE LEFIPSDDEI
     SDRVASDRGL TRPELSVLIA YGKMVLKDAL NIPEITDNPY HGKLLLQAFP EVLREKFSTH
     MQQHPLRSEI IATKLTNNMV NDMGLNFMFR IQEETGASVD DVANAYAIVH GIFDMETLWS
     RIEDLDNVIS AKLQLKMLDE ARRIMRRAAR WYIRHGNKAL SIEEAIACYR ETFNNLSKNL
     QNYLVEAEYS LLEEKTSTYV SQDVPKDIAY QVASFSNMFS SFDLAHVVAA EKRNVDVVAR
     LYFQLGSKLE LHWFLDQINN QAVSNHWQAL ARASYREELD WQQRSITANL LQINPEASDA
     DKILEDWMQS NQVLLKRWYH MMSEFKTSTT HEFAKFSVAL RELMLLSVKS SH
//