Tag | Content |
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CPLM ID | CPLM-002826 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glutamate synthase [NADPH] large chain |
Protein Synonyms/Alias | Glutamate synthase subunit alpha; GLTS alpha chain; NADPH-GOGAT |
Gene Name | gltB |
Gene Synonyms/Alias | aspB; b3212; JW3179 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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61 | GCGLLLQKPDRFFRI | acetylation | [1] | 79 | ERGWRLAKNYAVGML | acetylation | [1] | 90 | VGMLFLNKDPELAAA | acetylation | [1] | 172 | EKRLEADKDFYVCSL | acetylation | [1] | 365 | PARYVITKDKLITCA | acetylation | [1] | 417 | AETDDDLKSRHPYKE | acetylation | [1] | 423 | LKSRHPYKEWMEKNV | acetylation | [1] | 428 | PYKEWMEKNVRRLVP | acetylation | [1] | 459 | DTLASYQKQFNYSAE | acetylation | [1] | 553 | QAHRLSFKSPILLYS | acetylation | [1] | 563 | ILLYSDFKQLTTMKE | acetylation | [1] | 569 | FKQLTTMKEEHYRAD | acetylation | [1] | 594 | TTLEATVKELCDKAE | acetylation | [1] | 599 | TVKELCDKAEKMVRS | acetylation | [1] | 620 | LSDRNIAKDRLPVPA | acetylation | [1] | 693 | VDTHAIAKDYRTVML | acetylation | [1] | 708 | NYRNGINKGLYKIMS | acetylation | [1] | 712 | GINKGLYKIMSKMGI | acetylation | [1] | 769 | QDLLNLSKRAWLARK | acetylation | [1] | 776 | KRAWLARKPISQGGL | acetylation | [1] | 785 | ISQGGLLKYVHGGEY | acetylation | [1] | 820 | SDYQEYAKLVNERPA | acetylation | [1] | 856 | EPASELFKRFDTAAM | acetylation | [1] | 931 | NADVIQIKVAQGAKP | acetylation | [1] | 948 | GGQLPGDKVTPYIAK | acetylation | [1] | 955 | KVTPYIAKLRYSVPG | acetylation | [1] | 993 | DLKQVNPKAMISVKL | acetylation | [1] | 1123 | GVATQDDKLRKNHYH | acetylation | [1] | 1170 | IGRTDLLKELDGFTA | acetylation | [1] | 1186 | QQKLALSKLLETAEP | acetylation | [1] | 1197 | TAEPHPGKALYCTEN | acetylation | [1] | 1222 | AQLLQQAKPFVDERQ | acetylation | [1] | 1231 | FVDERQSKTFWFDIR | acetylation | [1] | 1456 | NWSTFATKFALVKPK | acetylation | [1] | 1461 | ATKFALVKPKSSDVK | acetylation | [1] | 1468 | KPKSSDVKALLGHRS | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | |
Sequence Annotation | DOMAIN 12 402 Glutamine amidotransferase type-2. NP_BIND 1049 1101 FMN (By similarity). ACT_SITE 12 12 For GATase activity (By similarity). METAL 1102 1102 Iron-sulfur (3Fe-4S) (By similarity). METAL 1108 1108 Iron-sulfur (3Fe-4S) (By similarity). METAL 1113 1113 Iron-sulfur (3Fe-4S) (By similarity). |
Keyword | 3Fe-4S; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1486 AA |
Protein Sequence | MLYDKSLERD NCGFGLIAHI EGEPSHKVVR TAIHALARMQ HRGAILADGK TGDGCGLLLQ 60 KPDRFFRIVA QERGWRLAKN YAVGMLFLNK DPELAAAARR IVEEELQRET LSIVGWRDVP 120 TNEGVLGEIA LSSLPRIEQI FVNAPAGWRP RDMERRLFIA RRRIEKRLEA DKDFYVCSLS 180 NLVNIYKGLC MPTDLPRFYL DLADLRLESA ICLFHQRFST NTVPRWPLAQ PFRYLAHNGE 240 INTITGNRQW ARARTYKFQT PLIPDLHDAA PFVNETGSDS SSMDNMLELL LAGGMDIIRA 300 MRLLVPPAWQ NNPDMDPELR AFFDFNSMHM EPWDGPAGIV MSDGRFAACN LDRNGLRPAR 360 YVITKDKLIT CASEVGIWDY QPDEVVEKGR VGPGELMVID TRSGRILHSA ETDDDLKSRH 420 PYKEWMEKNV RRLVPFEDLP DEEVGSRELD DDTLASYQKQ FNYSAEELDS VIRVLGENGQ 480 EAVGSMGDDT PFAVLSSQPR IIYDYFRQQF AQVTNPPIDP LREAHVMSLA TSIGREMNVF 540 CEAEGQAHRL SFKSPILLYS DFKQLTTMKE EHYRADTLDI TFDVTKTTLE ATVKELCDKA 600 EKMVRSGTVL LVLSDRNIAK DRLPVPAPMA VGAIQTRLVD QSLRCDANII VETASARDPH 660 HFAVLLGFGA TAIYPYLAYE TLGRLVDTHA IAKDYRTVML NYRNGINKGL YKIMSKMGIS 720 TIASYRCSKL FEAVGLHDDV VGLCFQGAVS RIGGASFEDF QQDLLNLSKR AWLARKPISQ 780 GGLLKYVHGG EYHAYNPDVV RTLQQAVQSG EYSDYQEYAK LVNERPATTL RDLLAITPGE 840 NAVNIADVEP ASELFKRFDT AAMSIGALSP EAHEALAEAM NSIGGNSNSG EGGEDPARYG 900 TNKVSRIKQV ASGRFGVTPA YLVNADVIQI KVAQGAKPGE GGQLPGDKVT PYIAKLRYSV 960 PGVTLISPPP HHDIYSIEDL AQLIFDLKQV NPKAMISVKL VSEPGVGTIA TGVAKAYADL 1020 ITIAGYDGGT GASPLSSVKY AGCPWELGLV ETQQALVANG LRHKIRLQVD GGLKTGVDII 1080 KAAILGAESF GFGTGPMVAL GCKYLRICHL NNCATGVATQ DDKLRKNHYH GLPFKVTNYF 1140 EFIARETREL MAQLGVTRLV DLIGRTDLLK ELDGFTAKQQ KLALSKLLET AEPHPGKALY 1200 CTENNPPFDN GLLNAQLLQQ AKPFVDERQS KTFWFDIRNT DRSVGASLSG YIAQTHGDQG 1260 LAADPIKAYF NGTAGQSFGV WNAGGVELYL TGDANDYVGK GMAGGLIAIR PPVGSAFRSH 1320 EASIIGNTCL YGATGGRLYA AGRAGERFGV RNSGAITVVE GIGDNGCEYM TGGIVCILGK 1380 TGVNFGAGMT GGFAYVLDES GDFRKRVNPE LVEVLSVDAL AIHEEHLRGL ITEHVQHTGS 1440 QRGEEILANW STFATKFALV KPKSSDVKAL LGHRSRSAAE LRVQAQ 1486 |
Gene Ontology | GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0004355; F:glutamate synthase (NADPH) activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006537; P:glutamate biosynthetic process; IDA:EcoCyc. GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway. |
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SMART | |
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PRINTS | |