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Database: UniProt
Entry: Q4UK71_RICFE
LinkDB: Q4UK71_RICFE
Original site: Q4UK71_RICFE 
ID   Q4UK71_RICFE            Unreviewed;      1594 AA.
AC   Q4UK71;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:AAY62064.1};
GN   OrderedLocusNames=RF_1213 {ECO:0000313|EMBL:AAY62064.1};
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456 {ECO:0000313|EMBL:AAY62064.1, ECO:0000313|Proteomes:UP000008548};
RN   [1] {ECO:0000313|EMBL:AAY62064.1, ECO:0000313|Proteomes:UP000008548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2 {ECO:0000313|Proteomes:UP000008548};
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.E.,
RA   Parinello H., Claverie J.M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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DR   EMBL; CP000053; AAY62064.1; -; Genomic_DNA.
DR   STRING; 315456.RF_1213; -.
DR   KEGG; rfe:RF_1213; -.
DR   eggNOG; COG2902; Bacteria.
DR   HOGENOM; CLU_003404_1_1_5; -.
DR   Proteomes; UP000008548; 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          51..174
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          404..492
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          557..613
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          720..1209
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1255..1585
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1594 AA;  182489 MW;  25EBE2F9F6DC90A6 CRC64;
     MIAYNIILEK IMPPKTTSLN FSRLNCQIPN YKTKILELSK ERESSSIYID FVQKFLNYIP
     IDYDFENREK LFQNFADEAF KFFKQRVERA RKIAITKTVI ENDPAINVLI LLDNKPHIVD
     FIICLLKNMN LQTKFLLHPV INCVRNSKGE LEKILENSVS DEKSESILHL TILGNFDDKT
     TTFLTEAINE RLEELEQSYS HLPQLLTKLQ GLSKNIIDND KLNFEEAKEF LNWLQNDNLV
     LLGTLDFEVK SIKLSNEIGA AKIWQEVKDE IDDIIKCSAN PLYQNQLIIL GKINSASLIH
     SDNLIDYILV KKFSSSGEYI SGSIIFGIYN SNMYYHSISD IPILRQKFNF VIEKAGFALS
     GYNADKLRIL MESLPREALI QIDQGDLYCM CLHMLSSMMS KKLKLFIQYD WSSSFLNIII
     FLPRERLTAE IHNMIDCYLA EKFGSKILSN YITEVVGNFS YLFVTLEAQG EHKINFEAEI
     IQQDLDRIST RWSEDFYFKL SKKFGEYQAG INLKLFDNVF PADYRQKFSP EIALVDIEYL
     TEASKSQECM FNLVSVNETE FYLKIYSPKV KLALSNILPP IENLGFKAID EQTFAIKEAL
     EIKESWIYNF ILTSIIPVKG NITELKINVE EALDQMALGM LANDSLSKLI VLAGFNWKQV
     KLVKALTRYL HQTGFSYGKG YVQLTLLKHP EYTKMLVNLF DIKFNPKHPD NNCGVIQDKL
     NNYLVTVEMS SEDKVLRSML GIINAITRTN YYQPHKHVFS FKFDSSKVPG LPKPVPFAEA
     FVYSKDFEAV HLRGGPVSRG GLRWSDRAED YRLEVLGLMK AQMTKNSVIV PVGSKGGFYV
     HFTEEGLTRD EYMEKVVECY KNFLRGLLDI TDNIVDGKVV HPKDVIIYDK EDPYLVVAAD
     KGTASFSDYA NSVSREYNYW LDDAFASGGS AGYDHKKMAI TSKGAWISVT NHFKTLGLDV
     QIDPITVVGI GDMSGDVFGN GMLRSEAIKL VAAFNHKHIF IDPTPDPVSS FNERLRLFNL
     KGSNWCDYDS KLISKGGKVF ERSSKLIKLS PEIKKLLDIN DNELSPEELI KAILKADVDL
     LWNGGIGTYI KAKTENNLEI GDKANDNLRC NGEEIRAKVI AEGGNVGVSQ RGRVEYAKKG
     GRINADFIDN SAGVDCSDHE VNIKIALSSA VTSGKITLEE RNKLLNDMTK QVEELVLLDN
     YKQTEAITIM QLSPTLTVNI LSQFIDILEE EKVLERENEF LPSAEELNRR AISGEVLTRP
     ELCVLLSYSK RSAYHELLNS TFSHDKYFDS YLIDYFPEMM QKKFRNEILS HPLKHEIIKT
     VTINKIINQL GGPLISIVKR EIGSPLCDII RSYTIICEIF DLDDIWETIS KLPTNIDYNV
     KIDMFTEITK LMRRGISWFI KNLKHPINIS ETIEEFRVPA QNLRKTVGTL LVGETKIRFE
     EKLNYYTTSG VEESFAATIA TFDNLISVFD TIYVTKQTSG NNKEIAKAYF AISDMFSLDW
     LRKACDKQLN DSFWRRLGIQ SLKDDLYDKQ RRLLIKIINK SKTTIDLDLW IDNNNNLVRN
     FLDFIKEIKS QETIDLNIII LANKKFEIFL QKLE
//
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