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Protein

Glutamate synthase [NADPH] small chain

Gene

gltD

Organism
Azospirillum brasilense
Status
Reviewed-Annotation score: Annotation score: 4 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] large chain (gltB), Glutamate synthase [NADPH] small chain (gltD)
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 bindingi95 – 951Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi99 – 991Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi105 – 1051Iron-sulfur (4Fe-4S)Sequence analysis
Metal bindingi109 – 1091Iron-sulfur (4Fe-4S)Sequence analysis

GO - Molecular functioni

GO - Biological processi

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

BioCyciMetaCyc:MONOMER-13080.
BRENDAi1.4.1.13. 611.
SABIO-RKQ05756.
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
OrganismiAzospirillum brasilense
Taxonomic identifieri192 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 482481Glutamate synthase [NADPH] small chainPRO_0000170799Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VDCelectron microscopy9.50G/H/I/J/K/L27-482[»]
ProteinModelPortaliQ05756.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05756.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 72344Fe-4S ferredoxin-typeAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

KOiK00266.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 1 hit.
InterProiIPR028261. 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.

Sequencei

Sequence statusi: Complete.

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

Q05756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANQRMLGFV HTAQRMPDKR PAAERRQDFA EIYARFSDER ANEQANRCSQ
60 70 80 90 100
CGVPFCQVHC PVSNNIPDWL KLTSEGRLEE AYEVSQATNN FPEICGRICP
110 120 130 140 150
QDRLCEGNCV IEQSTHGAVT IGSVEKYIND TAWDQGWVKP RTPSRELGLS
160 170 180 190 200
VGVIGAGPAG LAAAEELRAK GYEVHVYDRY DRMGGLLVYG IPGFKLEKSV
210 220 230 240 250
VERRVKLLAD AGVIYHPNFE VGRDASLPEL RRKHVAVLVA TGVYKARDIK
260 270 280 290 300
APGSGLGNIV AALDYLTTSN KVSLGDTVEA YENGSLNAAG KHVVVLGGGD
310 320 330 340 350
TAMDCVRTAI RQGATSVKCL YRRDRKNMPG SQREVAHAEE EGVEFIWQAA
360 370 380 390 400
PEGFTGDTVV TGVRAVRIHL GVADATGRQT PQVIEGSEFT VQADLVIKAL
410 420 430 440 450
GFEPEDLPNA FDEPELKVTR WGTLLVDHRT KMTNMDGVFA AGDIVRGASL
460 470 480
VVWAIRDGRD AAEGIHAYAK AKAEAPVAVA AE
Length:482
Mass (Da):52,358
Last modified:January 23, 2007 - v3
Checksum:i8224C1B4EAAFCB25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192408 Genomic DNA. Translation: AAG38999.1.
PIRiA46602.
RefSeqiWP_035677957.1. NZ_CP012915.1.

Genome annotation databases

KEGGiag:AAG38999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192408 Genomic DNA. Translation: AAG38999.1.
PIRiA46602.
RefSeqiWP_035677957.1. NZ_CP012915.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VDCelectron microscopy9.50G/H/I/J/K/L27-482[»]
ProteinModelPortaliQ05756.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAG38999.

Phylogenomic databases

KOiK00266.

Enzyme and pathway databases

UniPathwayiUPA00045.
UPA00634; UER00689.
BioCyciMetaCyc:MONOMER-13080.
BRENDAi1.4.1.13. 611.
SABIO-RKQ05756.

Miscellaneous databases

EvolutionaryTraceiQ05756.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 1 hit.
InterProiIPR028261. 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.
ProtoNetiSearch...

Publicationsi

  1. "Glutamate synthase genes of the diazotroph Azospirillum brasilense. Cloning, sequencing, and analysis of functional domains."
    Pelanda R., Vanoni M.A., Perego M., Piubelli L., Galizzi A., Curti B., Zanetti G.
    J. Biol. Chem. 268:3099-3106(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-24; 183-204 AND 328-344.
    Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.
  2. Vanoni M.A., Verzotti E., Morandi P., Curti B.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "Structural studies on the subunits of glutamate synthase from Azospirillum brasilense."
    Vanoni M.A., Negri A., Zanetti G., Ronchi S., Curti B.
    Biochim. Biophys. Acta 1039:374-377(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  4. "Interdomain loops and conformational changes of glutamate synthase as detected by limited proteolysis."
    Vanoni M.A., Mazzoni A., Fumagalli P., Negri A., Zanetti G., Curti B.
    Eur. J. Biochem. 226:505-515(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8.
    Strain: Sp6.

Entry informationi

Entry nameiGLTD_AZOBR
AccessioniPrimary (citable) accession number: Q05756
Secondary accession number(s): Q9EXL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 111 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

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.