ID W0BEL5_9GAMM Unreviewed; 1452 AA.
AC W0BEL5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:AHE67077.1};
DE EC=1.4.1.2 {ECO:0000313|EMBL:AHE67077.1};
GN ORFNames=Loa_01528 {ECO:0000313|EMBL:AHE67077.1};
OS Legionella oakridgensis ATCC 33761 = DSM 21215.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE67077.1, ECO:0000313|Proteomes:UP000018838};
RN [1] {ECO:0000313|EMBL:AHE67077.1, ECO:0000313|Proteomes:UP000018838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA Heuner K.;
RT "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT characterization reveals its replication capacity in amoebae.";
RL Int. J. Med. Microbiol. 303:514-528(2013).
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DR EMBL; CP004006; AHE67077.1; -; Genomic_DNA.
DR STRING; 1268635.Loa_01528; -.
DR KEGG; lok:Loa_01528; -.
DR PATRIC; fig|1268635.3.peg.1554; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_6; -.
DR Proteomes; UP000018838; 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 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 ECO:0000313|EMBL:AHE67077.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018838}.
FT DOMAIN 1..67
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 299..388
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 444..521
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 620..1114
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1159..1448
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1452 AA; 166798 MW; 25759CB37D3D09B6 CRC64;
MVVNRMGLAS HLIIHMGGVR LLRGKDNEVT AVLPQYDQTH PEAETDAPIF MEIDRQTDPH
VLDELYRNFE RVLEDNRVVV EDWALMREKV RTIIHELDTI STTLDANEVA ETKAFLNWIE
DHHFTFLGIR DYEIVEKDKE AILQAIPETG LGVLRQQLSK SKARSISTMT PEARELILSS
RILVMSKTNT LASVHRDAYT DYIGVKRFNK KGQVIGECRI IGLYTSAAYN TNPKHIPFLR
HKVAQIMKNS LLSPRSHAGK VLLNILETFP RDDLIQASED ELLEIAMGIF YMQERRRIRM
FARVDVYRRF ISCLVYVPRE RFNTELRQEM QEILRESFNA QEITFSTRFS ESILARIHFI
IRINPQESME FNFKEVEKKL IEVGRSWTDD LQQHLAEAFG EEKANRLYAQ YKDAFPAVYK
TNFPPRTAVF DIKHIEQLSK ENALSMNFYR PLDEFSDTFR LKIYQHDVTI PLSDVLPIIE
NLGMRAITER PYALKFDDEK ITWINDFAMQ YTRGNIFNFD DIRELFQNAF TSIWFGDAEN
DGFNQLVLAA GLDWRQVSVL RTYAKYFKQI GITFSQDYMV SALNNNTLLA KKLVQLFELH
FKPIKIKNRE SQIHGLVAEI LTDLDAVDNL DEDKIIRQYV QAITSTLRTN FYQLDDEGKY
KNYISIKLNS KTIAGVPRPY PMFEIFVYSP RLEGVHLRCG KVARGGIRWS DRKEDFRTEI
LGLMKAQQVK NAVIVPSGAK GGFVVKQLPL NGSREEIFAE GINCYKLFIR GLLDITDNYK
EGLIAKPTNV ICYDEDDPYL VVAADKGTAT FSDIANEISL KYGYWLGDAF ASGGSIGYDH
KKMGITAKGA WESVKRHFYE MGVDIETTDF TVVGIGDMAG DVFGNGMLLS KRIKLVAAFN
HMHIFIDPDP DPETSFKERQ RLFNLPRSTW ADYDKKLISK GGGVFNRNAK SIVVSKEMKQ
VFGIKQASVE PNELIRIVLQ ANVDLLWSAG IGTFVKAKSE TNAEVGDRTN DIIRINAKQL
RCKVIGEGGN LGLTQLARVE YALNGGLSYT DFIDNSAGVS CSDKEVNIKI LLNMIMTAGD
LTIKQRNELL VEMTDEVAHL VLRENFLQTR AISLMATQSL RSLELHSRYI NELERSGKLD
RRLEFLPDEK TLLERKLSGK GLSRPSMSVL FCYSKILLKE AILSSDVPED TYLKQLLVQS
FPEPLQVRFC EEMQHHPLKR EIIATKLSNI VVNEMGFSFV FRMQDETGAP VSAIVRAYMI
ARSVLDMETI WKQIDALSNQ IVAESQIEIM MMYVRLLRRL TRWFLRNQRK RLDISKAVKL
YGPGVEELKK SLPDILGENN RTKYERHYGK YKEMGLTEHL AHELAITRAL FAVLDIIEVA
HQSNVNISKV AEIYFNIGEF LELEWIRTQV IIHPTDDHWD ALSREALRDD LDWQQRQLTA
GIIQYDEKKK IL
//
