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Protein

Glutamate synthase [NADPH] small chain

Gene

gltD

Organism
Azospirillum brasilense
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

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

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)DescriptionActionsGraphical viewLength
Metal bindingi95Iron-sulfur (4Fe-4S)Sequence analysis1
Metal bindingi99Iron-sulfur (4Fe-4S)Sequence analysis1
Metal bindingi105Iron-sulfur (4Fe-4S)Sequence analysis1
Metal bindingi109Iron-sulfur (4Fe-4S)Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Glutamate biosynthesis
Ligand4Fe-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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001707992 – 482Glutamate synthase [NADPH] small chainAdd BLAST481

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VDCelectron microscopy9.50G/H/I/J/K/L27-482[»]
ProteinModelPortaliQ05756
SMRiQ05756
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05756

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 724Fe-4S ferredoxin-typeAdd BLAST34

Phylogenomic databases

KOiK00266

Family and domain databases

Gene3Di1.10.1060.10, 1 hit
3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR028261 DPD_II
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR006006 Glut_synth_ssu2
IPR009051 Helical_ferredxn
PfamiView protein in Pfam
PF14691 Fer4_20, 1 hit
PF07992 Pyr_redox_2, 1 hit
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_POQV01000012.1

Genome annotation databases

GeneIDi36111338
KEGGiag:AAG38999

Similar proteinsi

Entry informationi

Entry nameiGLTD_AZOBR
AccessioniPrimary (citable) accession number: Q05756
Secondary accession number(s): Q9EXL4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 120 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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