CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007189
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate synthase [NADPH] large chain 
Protein Synonyms/Alias
 NADPH-GOGAT 
Gene Name
 gltA 
Gene Synonyms/Alias
 BSU18450 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
159IGASSDLKDNLSFERacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
Functional Description
  
Sequence Annotation
 DOMAIN 22 415 Glutamine amidotransferase type-2.
 NP_BIND 1060 1112 FMN (By similarity).
 ACT_SITE 22 22 For GATase activity (By similarity).
 METAL 1113 1113 Iron-sulfur (3Fe-4S) (By similarity).
 METAL 1119 1119 Iron-sulfur (3Fe-4S) (By similarity).
 METAL 1124 1124 Iron-sulfur (3Fe-4S) (By similarity).  
Keyword
 3Fe-4S; Amino-acid biosynthesis; Complete proteome; FAD; Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1520 AA 
Protein Sequence
MTYNQMPKAQ GLYRPEFEHD ACGIGLYAHL KGKQTHDIVK QGLKMLCQLD HRGGQGSDPD 60
TGDGAGLLVQ IPDAFFRKEC KNINLPEKER YGVGMVFFSQ KEDERKKIEK QINALIEQEG 120
QVVLGWRTVP VNVGKIGTVA QKSCPFVRQV FIGASSDLKD NLSFERKLYV IRKQAENWGV 180
TEGLDFYFAS LSSQTIVYKG LLTPEQVDAF YSDLQDEAFV SAFALVHSRF STNTFPTWER 240
AHPNRYLVHN GEINTLRGNI NWMRAREQQF VSESFGEDLN KILPILNADG SDSSILDNAF 300
EFFVMAGRKP AHTAMMLIPE PWTENTHMSK EKRAFYEYHS SLMEPWDGPT AISFTDGKQI 360
GAILDRNGLR PARYYVTKDD YIIFSSEVGV IEVEQENVLY KNRLEPGKML LIDLEEGRII 420
SDEEVKTQIA TEYPYQKWLE EELVQVNPDP ESREEEQFSD LLTRQKAFGY TYEDIQKYLI 480
PVIKEGKDPL GSMGNDAPLA VLSDRAQSLF NYFKQLFAQV TNPPIDAIRE QLVTSTMTWL 540
GAEGDLLHPS ERNVRRIKLY TPVLSNEQFY ALKTIVHPDL KSQKIDVLFS EDLERGLKDM 600
FTQAEKAISQ GVSLLILSDK KMNERLTPIP PLLAVSALHQ HLIRKGLRTK VSIIVESGEA 660
REVHHFAALI GYGADAINPY LAYATYKQEI DEGRLDISYE EAVSKYGKSI TEGVVKVMSK 720
MGISTVQSYR GAQIFEAVGI SRDVIDRYFS GTASQLGGID LQTIAEEAQR RHREAYQDDY 780
SKTLEPGSDF QWRNGGEHHA FNPKTIHTLQ WACRRNDYNL FKQYTKAADE ERIGFLRNLF 840
AFDGNRKPLK LEEVESAESI VKRFKTGAMS FGSLSKEAHE ALAIAMNRLG GKSNSGEGGE 900
DPKRFVPDEN GDDRRSAIKQ IASGRFGVKS HYLVNADELQ IKMAQGAKPG EGGQLPGNKV 960
YPWVADVRGS TPGVGLISPP PHHDIYSIED LAQLIHDLKN ANRDARISVK LVSKAGVGTI 1020
AAGVAKATAD VIVISGYDGG TGASPKTSIK HTGLPWELGL AEAHQTLMLN GLRDRVVLET 1080
DGKLMTGRDV VMAALLGAEE FGFATAPLVV LGCVMMRACH LDTCPVGVAT QNPELRKKFM 1140
GDPDHIVNYM LFIAEEVREY MAALGFKTFD EMIGRTDVLH ASERAKEHWK ASQLDLSTLL 1200
YQPEGVRTFQ SPQNHKIDQS LDITTILPAV QEAIESGKEA DISIEINNTN RVAGTITGSE 1260
ISKRYGEEGL PEDTIKLHFT GSAGQSFGAF VPKGMTLYLD GDSNDYVGKG LSGGKIIVKS 1320
SEGFNSASDD NVIIGNVAFY GATSGEAYIN GRAGERFAVR NSGVNVVVEG IGDHGCEYMT 1380
GGSVVVLGDV GKNFAAGMSG GIAYVLTEDV KAFKRKCNLE MILFESLEDE KEIQQIKAML 1440
ERHTAYTNSQ KAEDLLDQWE DSVKKFVKVI PKNYKQMLAS IEEQKAAGLS DEEAIMFAFE 1500
ANTKPKQNTA ASGQKQAVVQ 1520 
Gene Ontology
 GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0004355; F:glutamate synthase (NADPH) activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
 GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR017932; GATase_2_dom.
 IPR000583; GATase_dom.
 IPR002489; Glu_synth_asu_C.
 IPR002932; Glu_synth_centr_C.
 IPR006982; Glu_synth_centr_N. 
Pfam
 PF00310; GATase_2
 PF04898; Glu_syn_central
 PF01645; Glu_synthase
 PF01493; GXGXG 
SMART
  
PROSITE
 PS51278; GATASE_TYPE_2 
PRINTS