Glutamate synthase [NADPH] small chain (P09832)

Identification
Name:Glutamate synthase [NADPH] small chain
Synonyms:
  • Glutamate synthase subunit beta
  • GLTS beta chain
  • NADPH-GOGAT
Gene Name:gltD
Enzyme Class:
Biological Properties
General Function:Involved in iron-sulfur cluster binding
Specific Function:2 L-glutamate + NADP(+) = L-glutamine + 2- oxoglutarate + NADPH
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 2.0Thumb+1.0Thumb
1.0alpha-Ketoglutarate + 1.0L-Glutamine + 1.0Hydrogen ion + 1.0NADPH → 2.0L-Glutamate + 1.0NADP
ReactionCard
2.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
2.0L-Glutamate + 1.0NAD ↔ 1.0L-Glutamine + 1.0alpha-Ketoglutarate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
2.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
2.0L-Glutamate + 1.0NADP ↔ 1.0L-Glutamine + 1.0alpha-Ketoglutarate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
2.0L-Glutamate + 1.0NADP + 1.0Ammonia + 1.0Water ↔ 1.0L-Glutamine + 1.0alpha-Ketoglutarate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
2.0L-Glutamic acid+1.0Thumb+2.0Thumb → 1.0Thumb+1.0NADPH+1.0Thumb+1.0Thumb+1.0Thumb
2.0L-Glutamic acid + 1.0NADP + 2.0L-Glutamate → 1.0L-Glutamine + 1.0NADPH + 1.0Hydrogen ion + 1.0Oxoglutaric acid + 1.0NADPH
ReactionCard
1.0Thumb+1.0Thumb+1.0NADPH+1.0Thumb+1.0Thumb → 2.0L-Glutamic acid+1.0Thumb+2.0Thumb
1.0L-Glutamine + 1.0Oxoglutaric acid + 1.0NADPH + 1.0Hydrogen ion + 1.0NADPH → 2.0L-Glutamic acid + 1.0NADP + 2.0L-Glutamate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB02812alpha-KetoglutarateMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
binding
catalytic activity
FAD or FADH2 binding
iron-sulfur cluster binding
metal cluster binding
nucleoside binding
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH2 group of donors
oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
purine nucleoside binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
glutamate biosynthetic process
glutamate metabolic process
glutamine family amino acid metabolic process
metabolic process
oxidation reduction
Gene Properties
Blattner:b3213
Gene OrientationClockwise
Centisome Percentage:72.36
Left Sequence End3357220
Right Sequence End3358638
Gene Sequence:
>1419 bp
ATGAGCCAGTCACTGTTTAGCCAACCATTGAACGTTATTAACGTCGGCATCGCCATGTTT
AGCGATGACCTGAAAAAGCAGCATGTAGAAGTGACTCAACTCGACTGGACGCCGCCGGGG
CAGGGCAATATGCAGGTGGTGCAGGCGCTGGATAACATTGCCGATTCGCCGCTGGCGGAC
AAAATCGCCGCCGCTAACCAGCAGGCGCTGGAGCGTATTATCCAGTCGCATCCGGTGCTG
ATTGGTTTTGATCAGGCGATTAACGTGGTGCCGGGCATGACGGCGAAAACCATTCTTCAC
GCCGGGCCGCCGATCACCTGGGAAAAAATGTGCGGCGCGATGAAAGGCGCGGTCACCGGA
GCGCTGGTGTTCGAAGGACTGGCGAAAGATCTCGACGAGGCGGCTGAACTGGCGGCTTCC
GGGGAGATCACCTTCTCGCCGTGTCACGAGCACGACTGCGTGGGATCGATGGCGGGTGTT
ACCTCGGCCTCGATGTTTATGCACATCGTAAAAAACAAAACCTACGGCAACATCGCTTAT
ACCAACATGAGCGAGCAGATGGCGAAGATTTTGCGTATGGGCGCTAACGACCAGAGCGTG
ATTGACCGCCTGAACTGGATGCGTGATGTGCAGGGACCAATACTGCGCGACGCGATGAAA
ATTATCGGCGAAATCGATCTGCGCTTAATGCTGGCGCAGGCGCTGCATATGGGCGATGAG
TGCCATAACCGCAATAACGCCGGGACGACACTGCTGATTCAGGCGCTGACGCCGGGGATT
ATTCAGGCGGGTTATTCCGTCGAGCAACAGCGCGAAGTGTTTGAGTTTGTCGCCAGCAGC
GACTACTTCTCCGGCCCGACGTGGATGGCGATGTGTAAAGCGGCGATGGATGCGGCGCAT
GGCATCGAATACAGCACCGTGGTCACCACCATGGCGCGTAACGGCGTCGAGTTCGGCCTG
CGGGTCAGCGGCCTGCCGGGGCAATGGTTTACCGGCCCGGCGCAGCAGGTGATCGGCCCG
ATGTTTGCCGGTTATAAGCCGGAAGATTCGGGGCTGGATATCGGCGACAGCGCCATCACC
GAAACCTACGGTATTGGCGGATTTGCTATGGCGACCGCGCCCGCTATCGTCGCGCTGGTG
GGCGGCACGGTGGAAGAAGCTATTGATTTCTCCCGTCAGATGCGCGAAATCACCCTCGGT
GAAAACCCCAACGTCACCATTCCGCTGCTCGGTTTTATGGGCGTGCCGTCGGCAATCGAC
ATCACCCGCGTGGGTAGCAGCGGCATTCTGCCGGTGATCAACACCGCCATCGCCCATAAA
GATGCGGGCGTCGGCATGATTGGCGCGGGCATTGTGCATCCACCTTTTGCCTGCTTCGAG
AAAGCCATTCTTGGCTGGTGCGAACGTTACGGCGTCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:472
Protein Molecular Weight:52015
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutamate synthase [NADPH] small chain
MSQNVYQFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCP
VHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDRLCEGSCTLNDEFGAVTIG
NIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPE
IGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVG
TYQSMRGGLENEDADGVYAALPFLIANTKQLMGFGETRDEPFVSMEGKRVVVLGGGDTAM
DCVRTSVRQGAKHVTCAYRRDEENMPGSRREVKNAREEGVEFKFNVQPLGIEVNGNGKVS
GVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHNMEWLAKHSVELDSQG
RIIAPEGSDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWLEV
References
External Links:
ResourceLink
Uniprot ID:P09832
Uniprot Name:GLTD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674464
Ecogene ID:EG10404
Ecocyc:EG10404
ColiBase:b3213
Kegg Gene:b3213
EchoBASE ID:EB0399
CCDB:GLTD_ECOLI
BacMap:16131103
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Gosset, G., Merino, E., Recillas, F., Oliver, G., Becerril, B., Bolivar, F. (1989). "Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12." Protein Seq Data Anal 2:9-16. Pubmed: 2643092
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Oliver, G., Gosset, G., Sanchez-Pescador, R., Lozoya, E., Ku, L. M., Flores, N., Becerril, B., Valle, F., Bolivar, F. (1987). "Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12." Gene 60:1-11. Pubmed: 3326786
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841