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Database: UniProt
Entry: H8LQ94_RICSL
LinkDB: H8LQ94_RICSL
Original site: H8LQ94_RICSL 
ID   H8LQ94_RICSL            Unreviewed;      1582 AA.
AC   H8LQ94;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:AFD20171.1};
GN   ORFNames=MC3_06545 {ECO:0000313|EMBL:AFD20171.1};
OS   Rickettsia slovaca str. D-CWPP.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=1105109 {ECO:0000313|EMBL:AFD20171.1, ECO:0000313|Proteomes:UP000007592};
RN   [1] {ECO:0000313|EMBL:AFD20171.1, ECO:0000313|Proteomes:UP000007592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D-CWPP (RSB) {ECO:0000313|Proteomes:UP000007592};
RA   Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003375; AFD20171.1; -; Genomic_DNA.
DR   RefSeq; WP_014273782.1; NC_017065.1.
DR   KEGG; rsw:MC3_06545; -.
DR   PATRIC; fig|1105109.3.peg.1380; -.
DR   HOGENOM; CLU_003404_1_1_5; -.
DR   Proteomes; UP000007592; 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; 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}.
FT   DOMAIN          40..163
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          393..481
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          546..603
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          709..1198
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1244..1573
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1582 AA;  181309 MW;  122B6656E4408FE5 CRC64;
     MTPKTTSLNF SRLNCQIPNY KTKILELSKE RESSSIYIDF VQKFLNYIPI DYDFENRAKL
     FQNFADEAFK FFKQRIARAR KIAITKAVIE NDPAINVLIL LDNKPHIVDF IICLLKNMNL
     HTKFLLHPVI NCVRNSKGEL EKILENSVSD EKSESILHLT ILGNFDDKTT TFLTEAINER
     LEKLEQSYSH LPQLRTKLQD LSKNIIDNYK LNFKEAKEFL NWLQNDNLVL LGTLDFEVKS
     LKLSNEIGAE KIWQEVKDEI DDIIKCSANP LYQNQLIILG KINSASLIHS DNLIDYILVK
     NFDSSGEYIS GSIIFGIYNS NMYYHSISNI PILRQKFNFV IEKAGFALSG YNADKLRILM
     ESLPREALIQ IDQGDLYCMC LHMLSSMMSK KLKLFIQYDW SSSFLNIIIF LPRERLTAEI
     HNMIDCYLAE KFGSKILSNY ITEVAGNFSY LFVTLEAQGE HKISFEAEII QQDLDRISTC
     WSEDFYFKFS KKFGEYQTGI NLKLFDNVFS ADYRQKFSPE IALVDIEYLT EASKSQKCMF
     NLVSVNETEF YLKIYSPKVK LALSNILPPI ENLGFKAIDE QTFAIKEALE IKESWIYNFI
     LTSIVPVKDN ITELKINVEE ALDKMALGML ANDSLSKLIV LAGFNWKQVK LVKALTRYLH
     QTGFSYGKGY VQLTLLKHPE YTKMLVNLFD IKFNPKHSDN NCDVIKDKLN NYLVTVEMSS
     EDKVLRNMLG IVNAITRTNY YQPHKHIFSF KFDSSKVPDL PKPVPFAEAF VYSRNFEAVH
     LRGGPVSRGG LRWSDRAEDY RLEVLGLMKA QMTKNSVIVP VGSKGGFYVH FTEEGLTRDE
     YMEKVVECYK NFLRGLLDIT DNIIDGKVVH PKDVIIYDKE DPYLVVAADK GTASFSDYAN
     SVAREYNYWL DDAFASGGSA GYDHKKMAIT SKGAWISVTN HFKTLGLDVQ KDPITVVGIG
     DMSGDVFGNG MLRSETIKLV AAFNHKHIFI DPTPDPLSSF NERLRLFNLK GSNWSDYDSK
     LISKGGKVFE RSSKLIKLSP EIKKLLDIND NELSPEELIK AILKAGVDLL WNGGIGTYIK
     AKTENNLEIG DKANDNLRCN GEEIRAKVIA EGGNVGVSQR GRVEYAKKGG RINADFIDNS
     AGVDCSDHEV NIKIALSSAI TSGKITLEER NKLLNDMTKQ VEELVLLDNY KQTEAITIMQ
     LSPTLTVNIL SQFIDILEEE KVLERENEFL PSAEELNSRA MSGEVLTRPE LCILLSYSKR
     SAYHELINST FSHDKYFDAY LIDYFPEMMQ KKFRNEILSH PLKHEIIKTV TINKIMNQLG
     GPLISIVKRE IGAPLCDIIR SYTIICEIFD LDDIWETISK LPTNIDYNVK IDMFTEITKL
     MRRGISWFIK NLKHPINISE TIEEFRVPAQ NLRKTVDTLL VGETKIRFEE KLNYYTTSGV
     EESLAATIAT FDNLISVFDI IYVTKQTSGN NKEIAKAYFV ISDMFSLDWL RKACDRQLND
     SFWRRLGIQS LKDDLYDKQR RLLIKIINKS KTTIDLDLWI DNNNLVRNLL DFIKEIKAQE
     TIDLNIIILA NKKFEIFLQK LE
//
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