CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011883
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate synthase [NADH] 
Protein Synonyms/Alias
 NADH-GOGAT 
Gene Name
 GLT1 
Gene Synonyms/Alias
 YDL171C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
133AVGNVFFKKNEKNNKacetylation[1]
197LVPLYDEKQPEFNETubiquitination[2]
964AMNRLGAKSNCGEGGubiquitination[2]
1100ASGVAKAKADHILVSubiquitination[2]
1721QWKLALDKLLETNNFubiquitination[2]
1923REKIQGKKVIVVGGGubiquitination[2]
2115KCAASVDKFLMDGTTubiquitination[2]
2139QRDYKLLKELASQV*ubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate. 
Sequence Annotation
 DOMAIN 54 455 Glutamine amidotransferase type-2.
 NP_BIND 1132 1189 FMN (By similarity).
 NP_BIND 1928 1942 NAD (Potential).
 ACT_SITE 54 54 For GATase activity (By similarity).
 METAL 1185 1185 Iron-sulfur (3Fe-4S) (By similarity).
 METAL 1191 1191 Iron-sulfur (3Fe-4S) (By similarity).
 METAL 1196 1196 Iron-sulfur (3Fe-4S) (By similarity).
 MOD_RES 2070 2070 Phosphothreonine.  
Keyword
 3Fe-4S; Amino-acid biosynthesis; Coiled coil; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Reference proteome; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2145 AA 
Protein Sequence
MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE HDACGVGFVA 60
NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL GIPHEFMKRE FKLDLDLDIP 120
EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF EDLAASFNLS VLGWRNVPVD STILGDVALS 180
REPTILQPLL VPLYDEKQPE FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK 240
GQLTPAQVYN YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN 300
KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL SLPEAVMMMV 360
PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC GAILDRNGLR PCRYYITSDD 420
RVICASEVGV IPIENSLVVQ KGKLKPGDLF LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS 480
KVIKLDDLLS KTANLVPKEF ISQDSLSLKV QSDPRLLANG YTFEQVTFLL TPMALTGKEA 540
LGSMGNDAPL ACLNENPVLL YDYFRQLFAQ VTNPPIDPIR EANVMSLECY VGPQGNLLEM 600
HSSQCDRLLL KSPILHWNEF QALKNIEAAY PSWSVAEIDI TFDKSEGLLG YTDTIDKITK 660
LASEAIDDGK KILIITDRKM GANRVSISSL IAISCIHHHL IRNKQRSQVA LILETGEARE 720
IHHFCVLLGY GCDGVYPYLA METLVRMNRE GLLRNVNNDN DTLEEGQILE NYKHAIDAGI 780
LKVMSKMGIS TLASYKGAQI FEALGLDNSI VDLCFTGTSS RIRGVTFEYL AQDAFSLHER 840
GYPSRQTISK SVNLPESGEY HFRDGGYKHV NEPTAIASLQ DTVRNKNDVS WQLYVKKEME 900
AIRDCTLRGL LELDFENSVS IPLEQVEPWT EIARRFASGA MSYGSISMEA HSTLAIAMNR 960
LGAKSNCGEG GEDAERSAVQ ENGDTMRSAI KQVASARFGV TSYYLSDADE IQIKIAQGAK 1020
PGEGGELPAH KVSKDIAKTR HSTPNVGLIS PPPHHDIYSI EDLKQLIYDL KCANPRAGIS 1080
VKLVSEVGVG IVASGVAKAK ADHILVSGHD GGTGAARWTS VKYAGLPWEL GLAETHQTLV 1140
LNDLRRNVVV QTDGQLRTGF DIAVAVLLGA ESFTLATVPL IAMGCVMLRR CHLNSCAVGI 1200
ATQDPYLRSK FKGQPEHVIN FFYYLIQDLR QIMAKLGFRT IDEMVGHSEK LKKRDDVNAK 1260
AINIDLSPIL TPAHVIRPGV PTKFTKKQDH KLHTRLDNKL IDEAEVTLDR GLPVNIDASI 1320
INTDRALGST LSYRVSKKFG EDGLPKDTVV VNIEGSAGQS FGAFLASGIT FILNGDANDY 1380
VGKGLSGGII VIKPPKDSKF KSDENVIVGN TCFYGATSGT AFISGSAGER FGVRNSGATI 1440
VVERIKGNNA FEYMTGGRAI VLSQMESLNA FSGATGGIAY CLTSDYDDFV GKINKDTVEL 1500
ESLCDPVEIA FVKNLIQEHW NYTQSDLAAR ILGNFNHYLK DFVKVIPTDY KKVLLKEKAE 1560
AAKAKAKATS EYLKKFRSNQ EVDDEVNTLL IANQKAKEQE KKKSITISNK ATLKEPKVVD 1620
LEDAVPDSKQ LEKNSERIEK TRGFMIHKRR HETHRDPRTR VNDWKEFTNP ITKKDAKYQT 1680
ARCMDCGTPF CLSDTGCPLS NIIPKFNELL FKNQWKLALD KLLETNNFPE FTGRVCPAPC 1740
EGACTLGIIE DPVGIKSVER IIIDNAFKEG WIKPCPPSTR TGFTVGVIGS GPAGLACADM 1800
LNRAGHTVTV YERSDRCGGL LMYGIPNMKL DKAIVQRRID LLSAEGIDFV TNTEIGKTIS 1860
MDELKNKHNA VVYAIGSTIP RDLPIKGREL KNIDFAMQLL ESNTKALLNK DLEIIREKIQ 1920
GKKVIVVGGG DTGNDCLGTS VRHGAASVLN FELLPEPPVE RAKDNPWPQW PRVMRVDYGH 1980
AEVKEHYGRD PREYCILSKE FIGNDEGEVT AIRTVRVEWK KSQSGVWQMV EIPNSEEIFE 2040
ADIILLSMGF VGPELINGND NEVKKTRRGT IATLDDSSYS IDGGKTFACG DCRRGQSLIV 2100
WAIQEGRKCA ASVDKFLMDG TTYLPSNGGI VQRDYKLLKE LASQV 2145 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0010181; F:FMN binding; IEA:InterPro.
 GO:0016040; F:glutamate synthase (NADH) activity; IDA:SGD.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0019676; P:ammonia assimilation cycle; IEP:SGD.
 GO:0006537; P:glutamate biosynthetic process; IEP:SGD.
 GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR012285; Fum_reductase_C.
 IPR017932; GATase_2_dom.
 IPR000583; GATase_dom.
 IPR002489; Glu_synth_asu_C.
 IPR002932; Glu_synth_centr_C.
 IPR006982; Glu_synth_centr_N.
 IPR012220; Glu_synth_euk.
 IPR006005; Glut_synth_ssu1.
 IPR009051; Helical_ferredxn.
 IPR016040; NAD(P)-bd_dom.
 IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
 IPR001327; Pyr_OxRdtase_NAD-bd_dom. 
Pfam
 PF00310; GATase_2
 PF04898; Glu_syn_central
 PF01645; Glu_synthase
 PF01493; GXGXG
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2 
SMART
  
PROSITE
 PS51278; GATASE_TYPE_2 
PRINTS