ID A0A098G4X5_9GAMM Unreviewed; 1626 AA.
AC A0A098G4X5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:CEG57044.1};
GN ORFNames=LFA_1637 {ECO:0000313|EMBL:CEG57044.1};
OS Legionella fallonii LLAP-10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG57044.1, ECO:0000313|Proteomes:UP000032430};
RN [1] {ECO:0000313|Proteomes:UP000032430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
RA Gomez-Valero L.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LN614827; CEG57044.1; -; Genomic_DNA.
DR RefSeq; WP_045095613.1; NZ_LN614827.1.
DR STRING; 1212491.LFA_1637; -.
DR KEGG; lfa:LFA_1637; -.
DR HOGENOM; CLU_003404_1_1_6; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000032430; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000032430}.
FT DOMAIN 35..179
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 411..500
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 556..633
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 733..1227
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1273..1609
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1626 AA; 186025 MW; 8BBE48D0FF05CA84 CRC64;
MSYKFEEGKD VIVNSVVDKI KRSMAGDQSE FCAEFAKQLY STVALEDLES WDVDDLYGAV
VNFWSLMNER KPHETKIRIY NPDFERHGWQ TTHTVVELIC DDMPFIVDSM RMVINRMGLA
SHLIIHMGGI NVRRDKNDHI CEVLPRSKTI DTNGVMQEAP IFMEIDRQTD PKILDKLHRN
FERVLEDNRV VYEDWEKMRA EVREAIVQLD NVPKIIEPNE VDETKAFLNW IEDHHFTFLG
MRDYELVAKG KETILQAIPH TGLGVLRDDL SKSSARSISA MTPEAQELTL SPRILVMSKT
NTLASVHRDA YTDYIGIKRF NAKGEVIGER RLIGLYTSAA YHTNPRHIPF LRHKVALIME
NSGLNPRSHS GKVLLNILET LPRDDLIQGS EDELLEICMG IFYMQERKRI RLFARMDVYR
RFISCLVYVP KDRYNTELRY AMQKILADSF NAEEITFSTL FPESVLARIH FIVKVDPKSC
PDYDIKEIEK KLIEIGRSWT DDLQHHLYDA YGEEQANALF AHYRDAFPVS YCDNFTPRTA
VYDIKHIEML TPEQSLGINF YRPLDESVNS FRLKVYQHGT TIPLSDVLPI LENLGLRAIS
ERPYVLKFED GSVTWINDFA MQYTKDFEFQ LDEIKELFQN AFAEVWFGKA ENDGFNQLVL
AAGLDWRQVA ILRTYAKYFK QIGSIFSQEY MEMALNNNVA IAKKLVKLFE IRCNPQYVGH
NREQAFDVLS VEILADLDNV SNLDEDKIIR QYVHAISATL RTNFYQVDKE GNPKDYISIK
LSSKNIPGVP KPHPMFEIFV YSPRFEGVHL RCGKVARGGL RWSDRREDFR TEILGLMKAQ
QVKNSVIVPS GAKGGFVPKH LPVNGTREEI LAEGIACYKL FIRALLDITD NYKEGRIVKP
ENVIPYDEDD PYLVVAADKG TATFSDIANS ISLEYGFWLG DAFASGGSVG YDHKKMGITA
KGAWESVKRH FYELNIDIQN DDFTVVGIGD MSGDVFGNGM LLSKHIKLIG AFNHVHIFVD
PNPDAEKSFK ERERLFNLPR SSWTDYDKKL ISKGGGVFNR SAKSIPVSAE MKKVFGLKQD
NIEPNELIKT ILKAKVDLLW SGGIGTYVKS STESNANVGD RTNDSTRVNA KLLRCKVVGE
GGNLGLTQLA RVEYTLQGGM VYTDFIDNSG GVNCSDKEVN IKILLDTIVT AGDLTPKQRN
ELLSEMTDEV AKLVLRDNFL QTRAISLSDS QALRSLELQS RYINELERSG KLDRNLEFLP
DDKALLERKL KGYGLGRPAI AVLMCYSKTI LKEQILASDV PEENYMNQIL TSAFPKPLQE
RFSKQMQDHP LRREIIATRL SNIIVNEMGF TFVYRLQDET GAPVSAIVKA YMIARTVLDL
ESIWRQIEEL GTKINAQLQV DMMMLYVRLS RRVTRWFLRS QRRSLDIGRT IQLYSQGVVE
LKKCMPTVFG EEVRVHFDEH YQERVAAGVT PTLAHELTVT RALFAAPDII EIAHTYGLKV
AKVAEVYYGI GEFLDLPWIR TQIIIHPTEN HWESLSREAL RDDLDWQQRQ LTAGILSDNG
KNKDLITRLE SWGTYHIALI ERWRYILTDL KASTVLTYTM FFVAIRELLD LTQTTLQSHS
KLEAVD
//
