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Protein

Glutamate synthase [NADPH] small chain

Gene

gltD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH.

Cofactori

[4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster.

Pathwayi: L-glutamate biosynthesis via GLT pathway

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route).
Proteins known to be involved in this subpathway in this organism are:
  1. Glutamate synthase [NADPH] small chain (gltD), Glutamate synthase [NADPH] large chain (gltB)
This subpathway is part of the pathway L-glutamate biosynthesis via GLT pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route), the pathway L-glutamate biosynthesis via GLT pathway and in Amino-acid biosynthesis.

Pathwayi: nitrogen metabolism

This protein is involved in the pathway nitrogen metabolism, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrogen metabolism and in Energy metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi98 – 981Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi104 – 1041Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi108 – 1081Iron-sulfur (4Fe-4S)Sequence analysis

GO - Molecular functioni

GO - Biological processi

  • glutamate biosynthetic process Source: EcoCyc
  • L-glutamate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Glutamate biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BioCyciEcoCyc:GLUSYNSMALL-MONOMER.
ECOL316407:JW3180-MONOMER.
MetaCyc:GLUSYNSMALL-MONOMER.
MOB3B:GLUSYNSMALL-MONOMER.
BRENDAi1.4.1.13. 2026.
UniPathwayiUPA00045.
UPA00634; UER00689.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate synthase [NADPH] small chain (EC:1.4.1.13)
Alternative name(s):
Glutamate synthase subunit beta
Short name:
GLTS beta chain
NADPH-GOGAT
Gene namesi
Name:gltD
Synonyms:aspB
Ordered Locus Names:b3213, JW3180
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10404. gltD.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 472471Glutamate synthase [NADPH] small chainPRO_0000170800Add
BLAST

Proteomic databases

PaxDbiP09832.
PRIDEiP09832.

2D gel databases

SWISS-2DPAGEP09832.

Interactioni

Subunit structurei

Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
gltBP098312EBI-544293,EBI-551179

Protein-protein interaction databases

BioGridi4262427. 185 interactions.
DIPiDIP-9803N.
IntActiP09832. 6 interactions.
MINTiMINT-1248739.
STRINGi511145.b3213.

Structurei

3D structure databases

ProteinModelPortaliP09832.
SMRiP09832. Positions 18-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 69324Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105BZ8. Bacteria.
COG0493. LUCA.
HOGENOMiHOG000031439.
InParanoidiP09832.
KOiK00266.
OMAiWKPDMSK.
OrthoDBiEOG6XSZQF.
PhylomeDBiP09832.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR028261. DPD_II.
IPR023753. FAD/NAD-binding_dom.
IPR006006. Glut_synth_ssu2.
IPR009051. Helical_ferredxn.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF14691. Fer4_20. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
TIGRFAMsiTIGR01318. gltD_gamma_fam. 1 hit.
PROSITEiPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09832-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQNVYQFID LQRVDPPKKP LKIRKIEFVE IYEPFSEGQA KAQADRCLSC
60 70 80 90 100
GNPYCEWKCP VHNYIPNWLK LANEGRIFEA AELSHQTNTL PEVCGRVCPQ
110 120 130 140 150
DRLCEGSCTL NDEFGAVTIG NIERYINDKA FEMGWRPDMS GVKQTGKKVA
160 170 180 190 200
IIGAGPAGLA CADVLTRNGV KAVVFDRHPE IGGLLTFGIP AFKLEKEVMT
210 220 230 240 250
RRREIFTGMG IEFKLNTEVG RDVQLDDLLS DYDAVFLGVG TYQSMRGGLE
260 270 280 290 300
NEDADGVYAA LPFLIANTKQ LMGFGETRDE PFVSMEGKRV VVLGGGDTAM
310 320 330 340 350
DCVRTSVRQG AKHVTCAYRR DEENMPGSRR EVKNAREEGV EFKFNVQPLG
360 370 380 390 400
IEVNGNGKVS GVKMVRTEMG EPDAKGRRRA EIVAGSEHIV PADAVIMAFG
410 420 430 440 450
FRPHNMEWLA KHSVELDSQG RIIAPEGSDN AFQTSNPKIF AGGDIVRGSD
460 470
LVVTAIAEGR KAADGIMNWL EV
Length:472
Mass (Da):52,015
Last modified:January 23, 2007 - v3
Checksum:iF188CE1086040433
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 5114GQAKA…CLSCG → ARPKRRLTAACRAA (PubMed:3326786).CuratedAdd
BLAST
Sequence conflicti123 – 1231E → K in AAA23905 (PubMed:3326786).Curated
Sequence conflicti174 – 1741V → C in AAA23905 (PubMed:3326786).Curated
Sequence conflicti257 – 27014VYAAL…ANTKQ → CTQRCRSSSPTPNS (PubMed:3326786).CuratedAdd
BLAST
Sequence conflicti312 – 3132KH → ND in AAA23905 (PubMed:3326786).Curated
Sequence conflicti376 – 40025GRRRA…IMAFG → ASPRGDRCRFRTYRTGRCGD HGVW in AAA23905 (PubMed:3326786).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18747 Genomic DNA. Translation: AAA23905.1.
U18997 Genomic DNA. Translation: AAA58015.1.
U00096 Genomic DNA. Translation: AAC76245.1.
AP009048 Genomic DNA. Translation: BAE77257.1.
PIRiG65112.
RefSeqiNP_417680.1. NC_000913.3.
WP_000081674.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76245; AAC76245; b3213.
BAE77257; BAE77257; BAE77257.
GeneIDi947723.
KEGGiecj:JW3180.
eco:b3213.
PATRICi32121848. VBIEscCol129921_3308.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18747 Genomic DNA. Translation: AAA23905.1.
U18997 Genomic DNA. Translation: AAA58015.1.
U00096 Genomic DNA. Translation: AAC76245.1.
AP009048 Genomic DNA. Translation: BAE77257.1.
PIRiG65112.
RefSeqiNP_417680.1. NC_000913.3.
WP_000081674.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP09832.
SMRiP09832. Positions 18-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262427. 185 interactions.
DIPiDIP-9803N.
IntActiP09832. 6 interactions.
MINTiMINT-1248739.
STRINGi511145.b3213.

2D gel databases

SWISS-2DPAGEP09832.

Proteomic databases

PaxDbiP09832.
PRIDEiP09832.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76245; AAC76245; b3213.
BAE77257; BAE77257; BAE77257.
GeneIDi947723.
KEGGiecj:JW3180.
eco:b3213.
PATRICi32121848. VBIEscCol129921_3308.

Organism-specific databases

EchoBASEiEB0399.
EcoGeneiEG10404. gltD.

Phylogenomic databases

eggNOGiENOG4105BZ8. Bacteria.
COG0493. LUCA.
HOGENOMiHOG000031439.
InParanoidiP09832.
KOiK00266.
OMAiWKPDMSK.
OrthoDBiEOG6XSZQF.
PhylomeDBiP09832.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00689.
BioCyciEcoCyc:GLUSYNSMALL-MONOMER.
ECOL316407:JW3180-MONOMER.
MetaCyc:GLUSYNSMALL-MONOMER.
MOB3B:GLUSYNSMALL-MONOMER.
BRENDAi1.4.1.13. 2026.

Miscellaneous databases

PROiP09832.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR028261. DPD_II.
IPR023753. FAD/NAD-binding_dom.
IPR006006. Glut_synth_ssu2.
IPR009051. Helical_ferredxn.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF14691. Fer4_20. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
TIGRFAMsiTIGR01318. gltD_gamma_fam. 1 hit.
PROSITEiPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12."
    Oliver G., Gosset G., Sanchez-Pescador R., Lozoya E., Ku L.M., Flores N., Becerril B., Valle F., Bolivar F.
    Gene 60:1-11(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  5. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12."
    Gosset G., Merino E., Recillas F., Oliver G., Becerril B., Bolivar F.
    Protein Seq. Data Anal. 2:9-16(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiGLTD_ECOLI
AccessioniPrimary (citable) accession number: P09832
Secondary accession number(s): Q2M8Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Glutamine binds to the large subunit and transfers the amido group to 2-oxo-glutamate that apparently binds to the small subunit.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.